Phase Separation: Linking Cellular Compartmentalization to Disease

Eukaryotic cells are complex structures capable of coordinating numerous biochemical reactions in space and time. Key to such coordination is the subdivision of intracellular space into functional compartments. Compartmentalization can be achieved by intracellular membranes, which surround organelle...

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Published in:	Trends in cell biology Vol. 26; no. 7; pp. 547 - 558
Main Authors:	Aguzzi, Adriano, Altmeyer, Matthias
Format:	Journal Article
Language:	English
Published:	England Elsevier Ltd 01.07.2016
Subjects:	Animals Cell Compartmentation Disease Eukaryotic Cells - metabolism Humans intrinsically disordered proteins liquid demixing low-complexity domains neurodegeneration Pathology Phase Transition protein assembly and aggregation Proteins - metabolism neurodegeneration phase transition intrinsically disordered proteins liquid demixing low-complexity domains protein assembly and aggregation
ISSN:	0962-8924, 1879-3088
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Abstract	Eukaryotic cells are complex structures capable of coordinating numerous biochemical reactions in space and time. Key to such coordination is the subdivision of intracellular space into functional compartments. Compartmentalization can be achieved by intracellular membranes, which surround organelles and act as physical barriers. In addition, cells have developed sophisticated mechanisms to partition their inner substance in a tightly regulated manner. Recent studies provide compelling evidence that membraneless compartmentalization can be achieved by liquid demixing, a process culminating in liquid–liquid phase separation and the formation of phase boundaries. We discuss how this emerging concept may help in understanding dynamic reorganization of subcellular space and highlight its potential as a framework to explain pathological protein assembly in cancer and neurodegeneration. Membraneless compartmentalization of the subcellular space occurs by liquid–liquid phase separation. Heterotypic cooperative weak interactions enable rapid rearrangements within liquid compartments. Intrinsically disordered proteins play important roles in phase transitions due to their structural plasticity and prion-like properties. Cells dynamically control the extent and duration of phase transitions. Molecular seeds such as RNA or poly(ADP-ribose) (PAR) can trigger phase transitions in a stimulus- and context-specific manner. Chaperones, disintegrase machineries, and post-translational modifications cooperate to control phase transitions. A continuum of aggregation propensities exists and cells employ an unanticipated broad range of material states in proteinaceous assemblies. These can progress into pathological aggregates associated with neurodegenerative diseases.
AbstractList	Eukaryotic cells are complex structures capable of coordinating numerous biochemical reactions in space and time. Key to such coordination is the subdivision of intracellular space into functional compartments. Compartmentalization can be achieved by intracellular membranes, which surround organelles and act as physical barriers. In addition, cells have developed sophisticated mechanisms to partition their inner substance in a tightly regulated manner. Recent studies provide compelling evidence that membraneless compartmentalization can be achieved by liquid demixing, a process culminating in liquid–liquid phase separation and the formation of phase boundaries. We discuss how this emerging concept may help in understanding dynamic reorganization of subcellular space and highlight its potential as a framework to explain pathological protein assembly in cancer and neurodegeneration. Eukaryotic cells are complex structures capable of coordinating numerous biochemical reactions in space and time. Key to such coordination is the subdivision of intracellular space into functional compartments. Compartmentalization can be achieved by intracellular membranes, which surround organelles and act as physical barriers. In addition, cells have developed sophisticated mechanisms to partition their inner substance in a tightly regulated manner. Recent studies provide compelling evidence that membraneless compartmentalization can be achieved by liquid demixing, a process culminating in liquid–liquid phase separation and the formation of phase boundaries. We discuss how this emerging concept may help in understanding dynamic reorganization of subcellular space and highlight its potential as a framework to explain pathological protein assembly in cancer and neurodegeneration. Membraneless compartmentalization of the subcellular space occurs by liquid–liquid phase separation. Heterotypic cooperative weak interactions enable rapid rearrangements within liquid compartments. Intrinsically disordered proteins play important roles in phase transitions due to their structural plasticity and prion-like properties. Cells dynamically control the extent and duration of phase transitions. Molecular seeds such as RNA or poly(ADP-ribose) (PAR) can trigger phase transitions in a stimulus- and context-specific manner. Chaperones, disintegrase machineries, and post-translational modifications cooperate to control phase transitions. A continuum of aggregation propensities exists and cells employ an unanticipated broad range of material states in proteinaceous assemblies. These can progress into pathological aggregates associated with neurodegenerative diseases.
Author	Aguzzi, Adriano Altmeyer, Matthias
Author_xml	– sequence: 1 givenname: Adriano surname: Aguzzi fullname: Aguzzi, Adriano organization: Institute of Neuropathology, University of Zurich, Schmelzbergstrasse 12, CH-8091 Zurich, Switzerland – sequence: 2 givenname: Matthias surname: Altmeyer fullname: Altmeyer, Matthias email: matthias.altmeyer@uzh.ch organization: Department of Molecular Mechanisms of Disease, University of Zurich, Winterthurerstrasse 190, CH-8057 Zurich, Switzerland
BackLink	https://www.ncbi.nlm.nih.gov/pubmed/27051975$$D View this record in MEDLINE/PubMed
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Cites_doi	10.7554/eLife.04591 10.1016/j.sbi.2011.03.011 10.1038/nn.3514 10.1083/jcb.201404124 10.1016/j.molcel.2015.10.006 10.1038/nrm4032 10.1016/j.cell.2015.07.047 10.1016/j.celrep.2013.11.017 10.1126/science.1227157 10.1016/j.molcel.2015.06.012 10.1038/nature12481 10.1016/S0092-8674(03)01031-6 10.1016/j.brainres.2012.01.016 10.1016/j.molcel.2015.01.013 10.1038/nrm3920 10.1073/pnas.1504822112 10.1073/pnas.1404855111 10.1016/j.neuron.2015.10.030 10.1038/nature15369 10.1038/nature10879 10.1016/j.cell.2013.05.037 10.1038/ncomms7116 10.1016/j.bbapap.2013.01.003 10.1016/j.molcel.2013.05.021 10.1126/science.aad2033 10.1016/j.cub.2015.11.065 10.3389/fnagi.2015.00018 10.1080/19336896.2015.1020277 10.1016/j.cell.2012.04.017 10.1182/blood.V95.9.2748.009k31a_2748_2752 10.1126/science.1172046 10.1038/ncomms9088 10.1146/annurev-pathol-011110-130242 10.1038/nrg3813 10.1016/j.cell.2015.08.010 10.1038/nrm2873 10.1073/pnas.1109434108 10.1093/nar/gkv679 10.1126/science.1223728 10.1016/j.cell.2009.02.044 10.1016/j.cub.2011.06.002 10.1146/annurev-biochem-060614-034506 10.1016/j.ceb.2015.04.003 10.1016/j.cell.2013.07.038 10.1016/j.celrep.2014.09.040 10.1016/j.cancergen.2011.07.008 10.1016/j.cell.2015.12.038 10.1038/nphys3532 10.1101/cshperspect.a000711 10.1016/j.molcel.2015.01.037 10.1038/nrn3430 10.1016/j.celrep.2013.09.043 10.1016/j.freeradbiomed.2014.10.820 10.1083/jcb.201308087 10.1126/science.1254917 10.1038/nature13999 10.1016/j.molcel.2015.09.006 10.7554/eLife.04123 10.1016/j.devcel.2015.11.014 10.1083/jcb.201507052 10.1083/jcb.201402114 10.1016/j.cell.2015.08.060 10.4161/15548627.2014.994400 10.1038/nrm3884 10.1016/j.cell.2012.05.022 10.1016/j.tcb.2014.05.003 10.7554/eLife.04251 10.1038/srep16607 10.4161/nucl.1.1.10680 10.1038/nchembio.1931 10.1038/nature11922 10.1146/annurev-biochem-060614-034325 10.1093/nar/gkv1383 10.1152/physrev.00006.2009 10.1073/pnas.1017150108 10.1016/j.cell.2012.07.019 10.1016/j.tibs.2007.10.003 10.1016/j.tcb.2015.08.007 10.1016/j.cell.2015.01.052 10.1038/nrneurol.2014.78 10.1038/nrm3660 10.1016/j.cell.2015.10.040 10.1016/j.devcel.2011.06.013 10.1038/ncb2830 10.1016/j.cell.2013.01.033 10.1038/ncb2157 10.1016/j.neuron.2013.07.033 10.1016/j.ccell.2015.12.002 10.1093/nar/gkt835 10.1155/2011/837474 10.1073/pnas.1509317112 10.1016/j.cell.2015.09.015 10.1016/j.molcel.2015.06.006 10.1038/nrm3373 10.1083/jcb.201504117 10.1016/j.cell.2013.10.033 10.1016/j.cell.2015.03.032 10.1016/j.molcel.2015.08.018 10.1016/j.molcel.2015.09.017 10.1016/j.cub.2015.01.012 10.1101/gad.234591.113 10.1016/j.celrep.2015.04.061 10.1146/annurev-cellbio-100913-013325 10.7554/eLife.06807 10.1016/j.cell.2015.08.041 10.1083/jcb.201302044 10.1016/j.cell.2012.04.016
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PublicationTitle	Trends in cell biology
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References	Schwartz (bib0195) 2015; 84 Jackrel (bib0535) 2015; 9 Zwicker (bib0130) 2014; 111 Brangwynne (bib0245) 2015; 11 Morimoto (bib0360) 2015; 6 Altmeyer (bib0135) 2015; 6 Zhu (bib0040) 2015; 34 Malinovska (bib0050) 2013; 1834 Berchowitz (bib0405) 2015; 163 Banjade (bib0150) 2014 Burke (bib0330) 2015; 60 Bah (bib0315) 2015; 519 Elbaum-Garfinkle (bib0480) 2015; 35 Ling (bib0460) 2013; 79 Hottiger (bib0270) 2015; 84 Robberecht (bib0430) 2013; 14 Babu (bib0335) 2011; 21 King (bib0065) 2012; 1462 Wang (bib0320) 2014; 3 Jaunmuktane (bib0525) 2015; 525 Ciryam (bib0470) 2013; 5 Walther (bib0415) 2015; 161 Couthouis (bib0215) 2011; 108 Kroschwald (bib0390) 2015; 4 Wallace (bib0400) 2015; 162 Wang (bib0250) 2015; 43 Shevtsov (bib0180) 2011; 13 Guo (bib0310) 2015; 60 Frontzek (bib0530) 2016; 146 Hulsmann (bib0155) 2012; 150 Jucker (bib0510) 2013; 501 Schmidt (bib0160) 2015 Brangwynne (bib0005) 2009; 324 Svetoni (bib0485) 2014; 75 Courchaine (bib0105) 2015; 210 Thandapani (bib0340) 2013; 50 Li (bib0055) 2012; 483 Hyman (bib0120) 2011; 21 Jiang (bib0295) 2015; 163 Luk (bib0520) 2012; 338 Han (bib0015) 2012; 149 Ramaswami (bib0060) 2013; 154 Jain (bib0370) 2016; 164 Feric (bib0080) 2013; 15 Hyman (bib0035) 2014; 30 Hyman (bib0025) 2012; 337 Schwartz (bib0190) 2013; 5 Hudson (bib0260) 2014; 15 Gerstberger (bib0345) 2014; 15 Hipp (bib0365) 2014; 24 Li (bib0075) 2013; 201 Woerner (bib0490) 2016; 351 Zhong (bib0350) 2000; 95 Deng (bib0210) 2014; 10 Nott (bib0175) 2015; 57 Doyle (bib0375) 2013; 14 Wright (bib0045) 2015; 16 Kwon (bib0325) 2013; 155 Yang (bib0395) 2015; 11 Alberti (bib0070) 2009; 137 Feric (bib0085) 2015; 5 Kim (bib0450) 2013; 495 Molliex (bib0090) 2015; 163 Gonczy (bib0290) 2012; 13 Kwon (bib0495) 2014; 345 Wippich (bib0095) 2013; 152 Lui (bib0110) 2014; 9 Kraus (bib0265) 2015; 58 Aguzzi (bib0440) 2004; 116 Guerreiro (bib0445) 2015; 160 Drisaldi (bib0355) 2015; 11 Hennig (bib0100) 2015; 210 Berry (bib0225) 2015; 112 Wang (bib0505) 2013; 16 Brundin (bib0420) 2010; 11 Toretsky (bib0465) 2014; 206 Grob (bib0230) 2014; 28 Bock (bib0275) 2015; 58 Weber (bib0030) 2012; 149 Jankowsky (bib0255) 2015; 16 Aguzzi (bib0515) 2016; 26 Elbaum-Garfinkle (bib0240) 2015; 112 Dundr (bib0185) 2010; 2 Daniels (bib0280) 2015; 58 Strzelecka (bib0125) 2010; 1 Shulman (bib0425) 2011; 6 Xiang (bib0410) 2015; 163 Poepsel (bib0385) 2015; 11 Soragni (bib0540) 2016; 29 Brangwynne (bib0010) 2011; 108 Decker (bib0300) 2011; 21 Lin (bib0220) 2015; 60 Falahati (bib0235) 2016; 26 Tompa (bib0165) 2008; 33 Patel (bib0145) 2015; 162 Leung (bib0285) 2014; 205 Sankar (bib0200) 2011; 204 Rulten (bib0500) 2014; 42 Buchan (bib0380) 2013; 153 Kato (bib0020) 2012; 149 Aguzzi (bib0435) 2009; 89 Brangwynne (bib0115) 2013; 203 Kovar (bib0205) 2011; 2011 Murakami (bib0475) 2015; 88 Teloni (bib0140) 2016; 44 Uversky (bib0455) 2015; 7 Weber (bib0170) 2015; 25 Zhang (bib0305) 2015; 60 Brangwynne (10.1016/j.tcb.2016.03.004_bib0005) 2009; 324 Aguzzi (10.1016/j.tcb.2016.03.004_bib0440) 2004; 116 Ramaswami (10.1016/j.tcb.2016.03.004_bib0060) 2013; 154 King (10.1016/j.tcb.2016.03.004_bib0065) 2012; 1462 Daniels (10.1016/j.tcb.2016.03.004_bib0280) 2015; 58 Zhong (10.1016/j.tcb.2016.03.004_bib0350) 2000; 95 Brundin (10.1016/j.tcb.2016.03.004_bib0420) 2010; 11 Li (10.1016/j.tcb.2016.03.004_bib0055) 2012; 483 Aguzzi (10.1016/j.tcb.2016.03.004_bib0435) 2009; 89 Xiang (10.1016/j.tcb.2016.03.004_bib0410) 2015; 163 Woerner (10.1016/j.tcb.2016.03.004_bib0490) 2016; 351 Schwartz (10.1016/j.tcb.2016.03.004_bib0190) 2013; 5 Kim (10.1016/j.tcb.2016.03.004_bib0450) 2013; 495 Shulman (10.1016/j.tcb.2016.03.004_bib0425) 2011; 6 Grob (10.1016/j.tcb.2016.03.004_bib0230) 2014; 28 Wang (10.1016/j.tcb.2016.03.004_bib0505) 2013; 16 Brangwynne (10.1016/j.tcb.2016.03.004_bib0010) 2011; 108 Zhu (10.1016/j.tcb.2016.03.004_bib0040) 2015; 34 Weber (10.1016/j.tcb.2016.03.004_bib0030) 2012; 149 Burke (10.1016/j.tcb.2016.03.004_bib0330) 2015; 60 Teloni (10.1016/j.tcb.2016.03.004_bib0140) 2016; 44 Guo (10.1016/j.tcb.2016.03.004_bib0310) 2015; 60 Gonczy (10.1016/j.tcb.2016.03.004_bib0290) 2012; 13 Malinovska (10.1016/j.tcb.2016.03.004_bib0050) 2013; 1834 Berry (10.1016/j.tcb.2016.03.004_bib0225) 2015; 112 Kwon (10.1016/j.tcb.2016.03.004_bib0325) 2013; 155 Gerstberger (10.1016/j.tcb.2016.03.004_bib0345) 2014; 15 Doyle (10.1016/j.tcb.2016.03.004_bib0375) 2013; 14 Jucker (10.1016/j.tcb.2016.03.004_bib0510) 2013; 501 Hipp (10.1016/j.tcb.2016.03.004_bib0365) 2014; 24 Lui (10.1016/j.tcb.2016.03.004_bib0110) 2014; 9 Hudson (10.1016/j.tcb.2016.03.004_bib0260) 2014; 15 Jackrel (10.1016/j.tcb.2016.03.004_bib0535) 2015; 9 Sankar (10.1016/j.tcb.2016.03.004_bib0200) 2011; 204 Elbaum-Garfinkle (10.1016/j.tcb.2016.03.004_bib0240) 2015; 112 Patel (10.1016/j.tcb.2016.03.004_bib0145) 2015; 162 Zwicker (10.1016/j.tcb.2016.03.004_bib0130) 2014; 111 Morimoto (10.1016/j.tcb.2016.03.004_bib0360) 2015; 6 Brangwynne (10.1016/j.tcb.2016.03.004_bib0115) 2013; 203 Falahati (10.1016/j.tcb.2016.03.004_bib0235) 2016; 26 Buchan (10.1016/j.tcb.2016.03.004_bib0380) 2013; 153 Jain (10.1016/j.tcb.2016.03.004_bib0370) 2016; 164 Kwon (10.1016/j.tcb.2016.03.004_bib0495) 2014; 345 Leung (10.1016/j.tcb.2016.03.004_bib0285) 2014; 205 Ciryam (10.1016/j.tcb.2016.03.004_bib0470) 2013; 5 Luk (10.1016/j.tcb.2016.03.004_bib0520) 2012; 338 Jiang (10.1016/j.tcb.2016.03.004_bib0295) 2015; 163 Bock (10.1016/j.tcb.2016.03.004_bib0275) 2015; 58 Babu (10.1016/j.tcb.2016.03.004_bib0335) 2011; 21 Wallace (10.1016/j.tcb.2016.03.004_bib0400) 2015; 162 Hyman (10.1016/j.tcb.2016.03.004_bib0025) 2012; 337 Ling (10.1016/j.tcb.2016.03.004_bib0460) 2013; 79 Weber (10.1016/j.tcb.2016.03.004_bib0170) 2015; 25 Svetoni (10.1016/j.tcb.2016.03.004_bib0485) 2014; 75 Decker (10.1016/j.tcb.2016.03.004_bib0300) 2011; 21 Guerreiro (10.1016/j.tcb.2016.03.004_bib0445) 2015; 160 Schmidt (10.1016/j.tcb.2016.03.004_bib0160) 2015 Aguzzi (10.1016/j.tcb.2016.03.004_bib0515) 2016; 26 Jaunmuktane (10.1016/j.tcb.2016.03.004_bib0525) 2015; 525 Feric (10.1016/j.tcb.2016.03.004_bib0080) 2013; 15 Strzelecka (10.1016/j.tcb.2016.03.004_bib0125) 2010; 1 Hyman (10.1016/j.tcb.2016.03.004_bib0035) 2014; 30 Kovar (10.1016/j.tcb.2016.03.004_bib0205) 2011; 2011 Wang (10.1016/j.tcb.2016.03.004_bib0320) 2014; 3 Bah (10.1016/j.tcb.2016.03.004_bib0315) 2015; 519 Lin (10.1016/j.tcb.2016.03.004_bib0220) 2015; 60 Kato (10.1016/j.tcb.2016.03.004_bib0020) 2012; 149 Nott (10.1016/j.tcb.2016.03.004_bib0175) 2015; 57 Altmeyer (10.1016/j.tcb.2016.03.004_bib0135) 2015; 6 Han (10.1016/j.tcb.2016.03.004_bib0015) 2012; 149 Alberti (10.1016/j.tcb.2016.03.004_bib0070) 2009; 137 Kraus (10.1016/j.tcb.2016.03.004_bib0265) 2015; 58 Wright (10.1016/j.tcb.2016.03.004_bib0045) 2015; 16 Zhang (10.1016/j.tcb.2016.03.004_bib0305) 2015; 60 Elbaum-Garfinkle (10.1016/j.tcb.2016.03.004_bib0480) 2015; 35 Drisaldi (10.1016/j.tcb.2016.03.004_bib0355) 2015; 11 Walther (10.1016/j.tcb.2016.03.004_bib0415) 2015; 161 Poepsel (10.1016/j.tcb.2016.03.004_bib0385) 2015; 11 Murakami (10.1016/j.tcb.2016.03.004_bib0475) 2015; 88 Wang (10.1016/j.tcb.2016.03.004_bib0250) 2015; 43 Brangwynne (10.1016/j.tcb.2016.03.004_bib0245) 2015; 11 Berchowitz (10.1016/j.tcb.2016.03.004_bib0405) 2015; 163 Jankowsky (10.1016/j.tcb.2016.03.004_bib0255) 2015; 16 Dundr (10.1016/j.tcb.2016.03.004_bib0185) 2010; 2 Wippich (10.1016/j.tcb.2016.03.004_bib0095) 2013; 152 Hottiger (10.1016/j.tcb.2016.03.004_bib0270) 2015; 84 Couthouis (10.1016/j.tcb.2016.03.004_bib0215) 2011; 108 Kroschwald (10.1016/j.tcb.2016.03.004_bib0390) 2015; 4 Uversky (10.1016/j.tcb.2016.03.004_bib0455) 2015; 7 Feric (10.1016/j.tcb.2016.03.004_bib0085) 2015; 5 Courchaine (10.1016/j.tcb.2016.03.004_bib0105) 2015; 210 Robberecht (10.1016/j.tcb.2016.03.004_bib0430) 2013; 14 Frontzek (10.1016/j.tcb.2016.03.004_bib0530) 2016; 146 Rulten (10.1016/j.tcb.2016.03.004_bib0500) 2014; 42 Hulsmann (10.1016/j.tcb.2016.03.004_bib0155) 2012; 150 Li (10.1016/j.tcb.2016.03.004_bib0075) 2013; 201 Soragni (10.1016/j.tcb.2016.03.004_bib0540) 2016; 29 Schwartz (10.1016/j.tcb.2016.03.004_bib0195) 2015; 84 Yang (10.1016/j.tcb.2016.03.004_bib0395) 2015; 11 Hennig (10.1016/j.tcb.2016.03.004_bib0100) 2015; 210 Molliex (10.1016/j.tcb.2016.03.004_bib0090) 2015; 163 Tompa (10.1016/j.tcb.2016.03.004_bib0165) 2008; 33 Banjade (10.1016/j.tcb.2016.03.004_bib0150) 2014 Deng (10.1016/j.tcb.2016.03.004_bib0210) 2014; 10 Hyman (10.1016/j.tcb.2016.03.004_bib0120) 2011; 21 Shevtsov (10.1016/j.tcb.2016.03.004_bib0180) 2011; 13 Thandapani (10.1016/j.tcb.2016.03.004_bib0340) 2013; 50 Toretsky (10.1016/j.tcb.2016.03.004_bib0465) 2014; 206
References_xml	– volume: 163 start-page: 108 year: 2015 end-page: 122 ident: bib0295 article-title: Phase transition of spindle-associated protein regulate spindle apparatus assembly publication-title: Cell – volume: 112 start-page: 7189 year: 2015 end-page: 7194 ident: bib0240 article-title: The disordered P granule protein LAF-1 drives phase separation into droplets with tunable viscosity and dynamics publication-title: Proc. Natl. Acad. Sci. U.S.A. – volume: 84 start-page: 227 year: 2015 end-page: 263 ident: bib0270 article-title: Nuclear ADP-ribosylation and its role in chromatin plasticity, cell differentiation, and epigenetics publication-title: Annu. Rev. Biochem. – volume: 95 start-page: 2748 year: 2000 end-page: 2752 ident: bib0350 article-title: Role of SUMO-1-modified PML in nuclear body formation publication-title: Blood – volume: 137 start-page: 146 year: 2009 end-page: 158 ident: bib0070 article-title: A systematic survey identifies prions and illuminates sequence features of prionogenic proteins publication-title: Cell – volume: 155 start-page: 1049 year: 2013 end-page: 1060 ident: bib0325 article-title: Phosphorylation-regulated binding of RNA polymerase II to fibrous polymers of low-complexity domains publication-title: Cell – volume: 205 start-page: 613 year: 2014 end-page: 619 ident: bib0285 article-title: Poly(ADP-ribose): an organizer of cellular architecture publication-title: J. Cell Biol. – volume: 161 start-page: 919 year: 2015 end-page: 932 ident: bib0415 article-title: Widespread proteome remodeling and aggregation in aging publication-title: Cell – volume: 163 start-page: 123 year: 2015 end-page: 133 ident: bib0090 article-title: Phase separation by low complexity domains promotes stress granule assembly and drives pathological fibrillization publication-title: Cell – volume: 206 start-page: 579 year: 2014 end-page: 588 ident: bib0465 article-title: Assemblages: functional units formed by cellular phase separation publication-title: J. Cell Biol. – volume: 338 start-page: 949 year: 2012 end-page: 953 ident: bib0520 article-title: Pathological alpha-synuclein transmission initiates Parkinson-like neurodegeneration in nontransgenic mice publication-title: Science – volume: 146 start-page: w14287 year: 2016 ident: bib0530 article-title: Amyloid-beta pathology and cerebral amyloid angiopathy are frequent in iatrogenic Creutzfeldt–Jakob disease after dural grafting publication-title: Swiss Med. Wkly – volume: 60 start-page: 231 year: 2015 end-page: 241 ident: bib0330 article-title: Residue-by-residue view of publication-title: Mol. Cell – year: 2015 ident: bib0160 article-title: Nup98 FG domains from diverse species spontaneously phase-separate into particles with nuclear pore-like permselectivity publication-title: Elife – volume: 11 start-page: 899 year: 2015 end-page: 904 ident: bib0245 article-title: Polymer physics of intracellular phase transitions publication-title: Nat. Phys. – volume: 42 start-page: 307 year: 2014 end-page: 314 ident: bib0500 article-title: PARP-1 dependent recruitment of the amyotrophic lateral sclerosis-associated protein FUS/TLS to sites of oxidative DNA damage publication-title: Nucleic Acids Res. – volume: 5 start-page: 16607 year: 2015 ident: bib0085 article-title: Soft viscoelastic properties of nuclear actin age oocytes due to gravitational creep publication-title: Sci. Rep. – volume: 116 start-page: 313 year: 2004 end-page: 327 ident: bib0440 article-title: Mammalian prion biology: one century of evolving concepts publication-title: Cell – volume: 89 start-page: 1105 year: 2009 end-page: 1152 ident: bib0435 article-title: Prions: protein aggregation and infectious diseases publication-title: Physiol. Rev. – volume: 88 start-page: 678 year: 2015 end-page: 690 ident: bib0475 article-title: ALS/FTD mutation-induced phase transition of FUS liquid droplets and reversible hydrogels into irreversible hydrogels impairs RNP granule function publication-title: Neuron – volume: 111 start-page: E2636 year: 2014 end-page: E2645 ident: bib0130 article-title: Centrosomes are autocatalytic droplets of pericentriolar material organized by centrioles publication-title: Proc. Natl. Acad. Sci. U.S.A. – volume: 324 start-page: 1729 year: 2009 end-page: 1732 ident: bib0005 article-title: Germline P granules are liquid droplets that localize by controlled dissolution/condensation publication-title: Science – volume: 16 start-page: 533 year: 2015 end-page: 544 ident: bib0255 article-title: Specificity and nonspecificity in RNA–protein interactions publication-title: Nat. Rev. Mol. Cell Biol. – volume: 204 start-page: 351 year: 2011 end-page: 365 ident: bib0200 article-title: Promiscuous partnerships in Ewing's sarcoma publication-title: Cancer Genet. – volume: 519 start-page: 106 year: 2015 end-page: 109 ident: bib0315 article-title: Folding of an intrinsically disordered protein by phosphorylation as a regulatory switch publication-title: Nature – volume: 162 start-page: 1286 year: 2015 end-page: 1298 ident: bib0400 article-title: Reversible, specific, active aggregates of endogenous proteins assemble upon heat stress publication-title: Cell – volume: 26 start-page: 40 year: 2016 end-page: 51 ident: bib0515 article-title: Cell biology of prions and prionoids: a status report publication-title: Trends Cell Biol. – volume: 33 start-page: 2 year: 2008 end-page: 8 ident: bib0165 article-title: Fuzzy complexes: polymorphism and structural disorder in protein–protein interactions publication-title: Trends Biochem. Sci. – volume: 154 start-page: 727 year: 2013 end-page: 736 ident: bib0060 article-title: Altered ribostasis: RNA–protein granules in degenerative disorders publication-title: Cell – volume: 11 start-page: 214 year: 2015 end-page: 224 ident: bib0395 article-title: Poly-ADP-ribosylation of HMGB1 regulates TNFSF10/TRAIL resistance through autophagy publication-title: Autophagy – volume: 5 start-page: 918 year: 2013 end-page: 925 ident: bib0190 article-title: RNA seeds higher-order assembly of FUS protein publication-title: Cell Rep. – volume: 163 start-page: 829 year: 2015 end-page: 839 ident: bib0410 article-title: The LC domain of hnRNPA2 adopts similar conformations in hydrogel polymers, liquid-like droplets, and nuclei publication-title: Cell – volume: 162 start-page: 1066 year: 2015 end-page: 1077 ident: bib0145 article-title: A liquid-to-solid phase transition of the ALS protein FUS accelerated by disease mutation publication-title: Cell – volume: 16 start-page: 1383 year: 2013 end-page: 1391 ident: bib0505 article-title: Interaction of FUS and HDAC1 regulates DNA damage response and repair in neurons publication-title: Nat. Neurosci. – volume: 44 start-page: 993 year: 2016 end-page: 1006 ident: bib0140 article-title: Readers of poly(ADP-ribose): designed to be fit for purpose publication-title: Nucleic Acids Res. – volume: 149 start-page: 768 year: 2012 end-page: 779 ident: bib0015 article-title: Cell-free formation of RNA granules: bound RNAs identify features and components of cellular assemblies publication-title: Cell – volume: 13 start-page: 167 year: 2011 end-page: 173 ident: bib0180 article-title: Nucleation of nuclear bodies by RNA publication-title: Nat. Cell Biol. – volume: 351 start-page: 173 year: 2016 end-page: 176 ident: bib0490 article-title: Cytoplasmic protein aggregates interfere with nucleocytoplasmic transport of protein and RNA publication-title: Science – volume: 14 start-page: 617 year: 2013 end-page: 629 ident: bib0375 article-title: Protein rescue from aggregates by powerful molecular chaperone machines publication-title: Nat. Rev. Mol. Cell Biol. – volume: 60 start-page: 208 year: 2015 end-page: 219 ident: bib0220 article-title: Formation and maturation of phase-separated liquid droplets by RNA-binding proteins publication-title: Mol. Cell – volume: 11 start-page: 301 year: 2010 end-page: 307 ident: bib0420 article-title: Prion-like transmission of protein aggregates in neurodegenerative diseases publication-title: Nat. Rev. Mol. Cell Biol. – volume: 58 start-page: 902 year: 2015 end-page: 910 ident: bib0265 article-title: PARPs and ADP-ribosylation: 50 years..and counting publication-title: Mol. Cell – volume: 29 start-page: 90 year: 2016 end-page: 103 ident: bib0540 article-title: A designed inhibitor of p53 aggregation rescues p53 tumor suppression in ovarian carcinomas publication-title: Cancer Cell – volume: 153 start-page: 1461 year: 2013 end-page: 1474 ident: bib0380 article-title: Eukaryotic stress granules are cleared by autophagy and Cdc48/VCP function publication-title: Cell – volume: 15 start-page: 829 year: 2014 end-page: 845 ident: bib0345 article-title: A census of human RNA-binding proteins publication-title: Nat. Rev. Genet. – volume: 21 start-page: 14 year: 2011 end-page: 16 ident: bib0120 article-title: Beyond stereospecificity: liquids and mesoscale organization of cytoplasm publication-title: Dev. Cell – volume: 13 start-page: 425 year: 2012 end-page: 435 ident: bib0290 article-title: Towards a molecular architecture of centriole assembly publication-title: Nat. Rev. Mol. Cell Biol. – volume: 525 start-page: 247 year: 2015 end-page: 250 ident: bib0525 article-title: Evidence for human transmission of amyloid-beta pathology and cerebral amyloid angiopathy publication-title: Nature – volume: 3 start-page: e04591 year: 2014 ident: bib0320 article-title: Regulation of RNA granule dynamics by phosphorylation of serine-rich, intrinsically disordered proteins in publication-title: Elife – volume: 149 start-page: 1188 year: 2012 end-page: 1191 ident: bib0030 article-title: Getting RNA and protein in phase publication-title: Cell – volume: 25 start-page: 641 year: 2015 end-page: 646 ident: bib0170 article-title: Inverse size scaling of the nucleolus by a concentration-dependent phase transition publication-title: Curr. Biol. – volume: 108 start-page: 4334 year: 2011 end-page: 4339 ident: bib0010 article-title: Active liquid-like behavior of nucleoli determines their size and shape in publication-title: Proc. Natl. Acad. Sci. U.S.A. – volume: 11 start-page: 1694 year: 2015 end-page: 1702 ident: bib0355 article-title: SUMOylation is an inhibitory constraint that regulates the prion-like aggregation and activity of CPEB3 publication-title: Cell Rep. – volume: 34 start-page: 23 year: 2015 end-page: 30 ident: bib0040 article-title: Nuclear bodies: the emerging biophysics of nucleoplasmic phases publication-title: Curr. Opin. Cell Biol. – volume: 201 start-page: 361 year: 2013 end-page: 372 ident: bib0075 article-title: Stress granules as crucibles of ALS pathogenesis publication-title: J. Cell Biol. – volume: 4 start-page: e06807 year: 2015 ident: bib0390 article-title: Promiscuous interactions and protein disaggregases determine the material state of stress-inducible RNP granules publication-title: Elife – volume: 6 start-page: 193 year: 2011 end-page: 222 ident: bib0425 article-title: Parkinson's disease: genetics and pathogenesis publication-title: Annu. Rev. Pathol. – volume: 483 start-page: 336 year: 2012 end-page: 340 ident: bib0055 article-title: Phase transitions in the assembly of multivalent signalling proteins publication-title: Nature – volume: 5 start-page: 781 year: 2013 end-page: 790 ident: bib0470 article-title: Widespread aggregation and neurodegenerative diseases are associated with supersaturated proteins publication-title: Cell Rep. – volume: 150 start-page: 738 year: 2012 end-page: 751 ident: bib0155 article-title: The permeability of reconstituted nuclear pores provides direct evidence for the selective phase model publication-title: Cell – volume: 2 start-page: a000711 year: 2010 ident: bib0185 article-title: Biogenesis of nuclear bodies publication-title: Cold Spring Harb. Perspect. Biol. – volume: 6 start-page: 6116 year: 2015 ident: bib0360 article-title: The unexpected role of polyubiquitin chains in the formation of fibrillar aggregates publication-title: Nat. Commun. – volume: 75 start-page: S51 year: 2014 ident: bib0485 article-title: Oxidative stress affects FET proteins localization and alternative pre-mRNA processing in cellular models of ALS publication-title: Free Radic. Biol. Med. – volume: 16 start-page: 18 year: 2015 end-page: 29 ident: bib0045 article-title: Intrinsically disordered proteins in cellular signalling and regulation publication-title: Nat. Rev. Mol. Cell Biol. – volume: 58 start-page: 959 year: 2015 end-page: 969 ident: bib0275 article-title: RNA regulation by poly(ADP-ribose) polymerases publication-title: Mol. Cell – volume: 30 start-page: 39 year: 2014 end-page: 58 ident: bib0035 article-title: Liquid–liquid phase separation in biology publication-title: Annu. Rev. Cell Dev. Biol. – volume: 15 start-page: 749 year: 2014 end-page: 760 ident: bib0260 article-title: The structure, function and evolution of proteins that bind DNA and RNA publication-title: Nat. Rev. Mol. Cell Biol. – volume: 24 start-page: 506 year: 2014 end-page: 514 ident: bib0365 article-title: Proteostasis impairment in protein-misfolding and -aggregation diseases publication-title: Trends Cell Biol. – volume: 108 start-page: 20881 year: 2011 end-page: 20890 ident: bib0215 article-title: A yeast functional screen predicts new candidate ALS disease genes publication-title: Proc. Natl. Acad. Sci. U.S.A. – volume: 345 start-page: 1139 year: 2014 end-page: 1145 ident: bib0495 article-title: Poly-dipeptides encoded by the C9ORF72 repeats bind nucleoli, impede RNA biogenesis, and kill cells publication-title: Science – volume: 21 start-page: 1259 year: 2011 end-page: 1267 ident: bib0300 article-title: Limiting amounts of centrosome material set centrosome size in publication-title: Curr. Biol. – volume: 35 start-page: 531 year: 2015 end-page: 532 ident: bib0480 article-title: Liquids, fibers, and gels: the many phases of neurodegeneration publication-title: Dev. Cell – volume: 1462 start-page: 61 year: 2012 end-page: 80 ident: bib0065 article-title: The tip of the iceberg: RNA-binding proteins with prion-like domains in neurodegenerative disease publication-title: Brain Res. – volume: 11 start-page: 862 year: 2015 end-page: 869 ident: bib0385 article-title: Determinants of amyloid fibril degradation by the PDZ protease HTRA1 publication-title: Nat. Chem. Biol. – volume: 6 start-page: 8088 year: 2015 ident: bib0135 article-title: Liquid demixing of intrinsically disordered proteins is seeded by poly(ADP-ribose) publication-title: Nat. Commun. – volume: 160 start-page: 798 year: 2015 ident: bib0445 article-title: SnapShot: genetics of ALS and FTD publication-title: Cell – volume: 60 start-page: 189 year: 2015 end-page: 192 ident: bib0310 article-title: It's raining liquids: RNA tunes viscoelasticity and dynamics of membraneless organelles publication-title: Mol. Cell – volume: 14 start-page: 248 year: 2013 end-page: 264 ident: bib0430 article-title: The changing scene of amyotrophic lateral sclerosis publication-title: Nat. Rev. Neurosci. – volume: 337 start-page: 1047 year: 2012 end-page: 1049 ident: bib0025 article-title: Cell biology. Beyond oil and water – phase transitions in cells publication-title: Science – volume: 1834 start-page: 918 year: 2013 end-page: 931 ident: bib0050 article-title: Protein disorder, prion propensities, and self-organizing macromolecular collectives publication-title: Biochim. Biophys. Acta – volume: 43 start-page: 7535 year: 2015 end-page: 7543 ident: bib0250 article-title: Nucleic acid-binding specificity of human FUS protein publication-title: Nucleic Acids Res. – volume: 84 start-page: 355 year: 2015 end-page: 379 ident: bib0195 article-title: Biochemical properties and biological functions of FET proteins publication-title: Annu. Rev. Biochem. – volume: 15 start-page: 1253 year: 2013 end-page: 1259 ident: bib0080 article-title: A nuclear F-actin scaffold stabilizes ribonucleoprotein droplets against gravity in large cells publication-title: Nat. Cell Biol. – volume: 9 start-page: 944 year: 2014 end-page: 954 ident: bib0110 article-title: Granules harboring translationally active mRNAs provide a platform for P-body formation following stress publication-title: Cell Rep. – volume: 10 start-page: 337 year: 2014 end-page: 348 ident: bib0210 article-title: The role of FUS gene variants in neurodegenerative diseases publication-title: Nat. Rev. Neurol. – volume: 79 start-page: 416 year: 2013 end-page: 438 ident: bib0460 article-title: Converging mechanisms in ALS and FTD: disrupted RNA and protein homeostasis publication-title: Neuron – volume: 26 start-page: 277 year: 2016 end-page: 285 ident: bib0235 article-title: Nucleation by rRNA dictates the precision of nucleolus assembly publication-title: Curr. Biol. – volume: 9 start-page: 90 year: 2015 end-page: 109 ident: bib0535 article-title: Engineering enhanced protein disaggregases for neurodegenerative disease publication-title: Prion – year: 2014 ident: bib0150 article-title: Phase transitions of multivalent proteins can promote clustering of membrane receptors publication-title: Elife – volume: 1 start-page: 96 year: 2010 end-page: 108 ident: bib0125 article-title: Dynamic control of Cajal body number during zebrafish embryogenesis publication-title: Nucleus – volume: 58 start-page: 911 year: 2015 end-page: 924 ident: bib0280 article-title: The promise of proteomics for the study of ADP-ribosylation publication-title: Mol. Cell – volume: 501 start-page: 45 year: 2013 end-page: 51 ident: bib0510 article-title: Self-propagation of pathogenic protein aggregates in neurodegenerative diseases publication-title: Nature – volume: 203 start-page: 875 year: 2013 end-page: 881 ident: bib0115 article-title: Phase transitions and size scaling of membrane-less organelles publication-title: J. Cell Biol. – volume: 152 start-page: 791 year: 2013 end-page: 805 ident: bib0095 article-title: Dual specificity kinase DYRK3 couples stress granule condensation/dissolution to mTORC1 signaling publication-title: Cell – volume: 210 start-page: 527 year: 2015 end-page: 528 ident: bib0105 article-title: Paraspeckles: paragons of functional aggregation publication-title: J. Cell Biol. – volume: 57 start-page: 936 year: 2015 end-page: 947 ident: bib0175 article-title: Phase transition of a disordered nuage protein generates environmentally responsive membraneless organelles publication-title: Mol. Cell – volume: 163 start-page: 406 year: 2015 end-page: 418 ident: bib0405 article-title: Regulated formation of an amyloid-like translational repressor governs gametogenesis publication-title: Cell – volume: 112 start-page: E5237 year: 2015 end-page: E5245 ident: bib0225 article-title: RNA transcription modulates phase transition-driven nuclear body assembly publication-title: Proc. Natl. Acad. Sci. U.S.A. – volume: 210 start-page: 529 year: 2015 end-page: 539 ident: bib0100 article-title: Prion-like domains in RNA binding proteins are essential for building subnuclear paraspeckles publication-title: J. Cell Biol. – volume: 164 start-page: 487 year: 2016 end-page: 498 ident: bib0370 article-title: ATPase-modulated stress granules contain a diverse proteome and substructure publication-title: Cell – volume: 50 start-page: 613 year: 2013 end-page: 623 ident: bib0340 article-title: Defining the RGG/RG motif publication-title: Mol. Cell – volume: 2011 start-page: 837474 year: 2011 ident: bib0205 article-title: Dr Jekyll and Mr Hyde: the two faces of the FUS/EWS/TAF15 protein family publication-title: Sarcoma – volume: 495 start-page: 467 year: 2013 end-page: 473 ident: bib0450 article-title: Mutations in prion-like domains in hnRNPA2B1 and hnRNPA1 cause multisystem proteinopathy and ALS publication-title: Nature – volume: 21 start-page: 432 year: 2011 end-page: 440 ident: bib0335 article-title: Intrinsically disordered proteins: regulation and disease publication-title: Curr. Opin. Struct. Biol. – volume: 149 start-page: 753 year: 2012 end-page: 767 ident: bib0020 article-title: Cell-free formation of RNA granules: low complexity sequence domains form dynamic fibers within hydrogels publication-title: Cell – volume: 60 start-page: 220 year: 2015 end-page: 230 ident: bib0305 article-title: RNA controls polyQ protein phase transitions publication-title: Mol. Cell – volume: 28 start-page: 220 year: 2014 end-page: 230 ident: bib0230 article-title: Construction of synthetic nucleoli in human cells reveals how a major functional nuclear domain is formed and propagated through cell division publication-title: Genes Dev. – volume: 7 start-page: 18 year: 2015 ident: bib0455 article-title: Intrinsically disordered proteins and their (disordered) proteomes in neurodegenerative disorders publication-title: Front. Aging Neurosci. – volume: 3 start-page: e04591 year: 2014 ident: 10.1016/j.tcb.2016.03.004_bib0320 article-title: Regulation of RNA granule dynamics by phosphorylation of serine-rich, intrinsically disordered proteins in C. elegans publication-title: Elife doi: 10.7554/eLife.04591 – volume: 21 start-page: 432 year: 2011 ident: 10.1016/j.tcb.2016.03.004_bib0335 article-title: Intrinsically disordered proteins: regulation and disease publication-title: Curr. Opin. Struct. Biol. doi: 10.1016/j.sbi.2011.03.011 – volume: 16 start-page: 1383 year: 2013 ident: 10.1016/j.tcb.2016.03.004_bib0505 article-title: Interaction of FUS and HDAC1 regulates DNA damage response and repair in neurons publication-title: Nat. Neurosci. doi: 10.1038/nn.3514 – volume: 206 start-page: 579 year: 2014 ident: 10.1016/j.tcb.2016.03.004_bib0465 article-title: Assemblages: functional units formed by cellular phase separation publication-title: J. Cell Biol. doi: 10.1083/jcb.201404124 – volume: 60 start-page: 189 year: 2015 ident: 10.1016/j.tcb.2016.03.004_bib0310 article-title: It's raining liquids: RNA tunes viscoelasticity and dynamics of membraneless organelles publication-title: Mol. Cell doi: 10.1016/j.molcel.2015.10.006 – volume: 16 start-page: 533 year: 2015 ident: 10.1016/j.tcb.2016.03.004_bib0255 article-title: Specificity and nonspecificity in RNA–protein interactions publication-title: Nat. Rev. Mol. Cell Biol. doi: 10.1038/nrm4032 – volume: 162 start-page: 1066 year: 2015 ident: 10.1016/j.tcb.2016.03.004_bib0145 article-title: A liquid-to-solid phase transition of the ALS protein FUS accelerated by disease mutation publication-title: Cell doi: 10.1016/j.cell.2015.07.047 – volume: 5 start-page: 918 year: 2013 ident: 10.1016/j.tcb.2016.03.004_bib0190 article-title: RNA seeds higher-order assembly of FUS protein publication-title: Cell Rep. doi: 10.1016/j.celrep.2013.11.017 – volume: 338 start-page: 949 year: 2012 ident: 10.1016/j.tcb.2016.03.004_bib0520 article-title: Pathological alpha-synuclein transmission initiates Parkinson-like neurodegeneration in nontransgenic mice publication-title: Science doi: 10.1126/science.1227157 – volume: 58 start-page: 911 year: 2015 ident: 10.1016/j.tcb.2016.03.004_bib0280 article-title: The promise of proteomics for the study of ADP-ribosylation publication-title: Mol. Cell doi: 10.1016/j.molcel.2015.06.012 – volume: 501 start-page: 45 year: 2013 ident: 10.1016/j.tcb.2016.03.004_bib0510 article-title: Self-propagation of pathogenic protein aggregates in neurodegenerative diseases publication-title: Nature doi: 10.1038/nature12481 – volume: 116 start-page: 313 year: 2004 ident: 10.1016/j.tcb.2016.03.004_bib0440 article-title: Mammalian prion biology: one century of evolving concepts publication-title: Cell doi: 10.1016/S0092-8674(03)01031-6 – volume: 1462 start-page: 61 year: 2012 ident: 10.1016/j.tcb.2016.03.004_bib0065 article-title: The tip of the iceberg: RNA-binding proteins with prion-like domains in neurodegenerative disease publication-title: Brain Res. doi: 10.1016/j.brainres.2012.01.016 – volume: 57 start-page: 936 year: 2015 ident: 10.1016/j.tcb.2016.03.004_bib0175 article-title: Phase transition of a disordered nuage protein generates environmentally responsive membraneless organelles publication-title: Mol. Cell doi: 10.1016/j.molcel.2015.01.013 – volume: 16 start-page: 18 year: 2015 ident: 10.1016/j.tcb.2016.03.004_bib0045 article-title: Intrinsically disordered proteins in cellular signalling and regulation publication-title: Nat. Rev. Mol. Cell Biol. doi: 10.1038/nrm3920 – volume: 112 start-page: 7189 year: 2015 ident: 10.1016/j.tcb.2016.03.004_bib0240 article-title: The disordered P granule protein LAF-1 drives phase separation into droplets with tunable viscosity and dynamics publication-title: Proc. Natl. Acad. Sci. U.S.A. doi: 10.1073/pnas.1504822112 – volume: 111 start-page: E2636 year: 2014 ident: 10.1016/j.tcb.2016.03.004_bib0130 article-title: Centrosomes are autocatalytic droplets of pericentriolar material organized by centrioles publication-title: Proc. Natl. Acad. Sci. U.S.A. doi: 10.1073/pnas.1404855111 – volume: 88 start-page: 678 year: 2015 ident: 10.1016/j.tcb.2016.03.004_bib0475 article-title: ALS/FTD mutation-induced phase transition of FUS liquid droplets and reversible hydrogels into irreversible hydrogels impairs RNP granule function publication-title: Neuron doi: 10.1016/j.neuron.2015.10.030 – volume: 525 start-page: 247 year: 2015 ident: 10.1016/j.tcb.2016.03.004_bib0525 article-title: Evidence for human transmission of amyloid-beta pathology and cerebral amyloid angiopathy publication-title: Nature doi: 10.1038/nature15369 – volume: 483 start-page: 336 year: 2012 ident: 10.1016/j.tcb.2016.03.004_bib0055 article-title: Phase transitions in the assembly of multivalent signalling proteins publication-title: Nature doi: 10.1038/nature10879 – volume: 153 start-page: 1461 year: 2013 ident: 10.1016/j.tcb.2016.03.004_bib0380 article-title: Eukaryotic stress granules are cleared by autophagy and Cdc48/VCP function publication-title: Cell doi: 10.1016/j.cell.2013.05.037 – volume: 6 start-page: 6116 year: 2015 ident: 10.1016/j.tcb.2016.03.004_bib0360 article-title: The unexpected role of polyubiquitin chains in the formation of fibrillar aggregates publication-title: Nat. Commun. doi: 10.1038/ncomms7116 – volume: 1834 start-page: 918 year: 2013 ident: 10.1016/j.tcb.2016.03.004_bib0050 article-title: Protein disorder, prion propensities, and self-organizing macromolecular collectives publication-title: Biochim. Biophys. Acta doi: 10.1016/j.bbapap.2013.01.003 – volume: 50 start-page: 613 year: 2013 ident: 10.1016/j.tcb.2016.03.004_bib0340 article-title: Defining the RGG/RG motif publication-title: Mol. Cell doi: 10.1016/j.molcel.2013.05.021 – volume: 351 start-page: 173 year: 2016 ident: 10.1016/j.tcb.2016.03.004_bib0490 article-title: Cytoplasmic protein aggregates interfere with nucleocytoplasmic transport of protein and RNA publication-title: Science doi: 10.1126/science.aad2033 – volume: 26 start-page: 277 year: 2016 ident: 10.1016/j.tcb.2016.03.004_bib0235 article-title: Nucleation by rRNA dictates the precision of nucleolus assembly publication-title: Curr. Biol. doi: 10.1016/j.cub.2015.11.065 – volume: 7 start-page: 18 year: 2015 ident: 10.1016/j.tcb.2016.03.004_bib0455 article-title: Intrinsically disordered proteins and their (disordered) proteomes in neurodegenerative disorders publication-title: Front. Aging Neurosci. doi: 10.3389/fnagi.2015.00018 – volume: 9 start-page: 90 year: 2015 ident: 10.1016/j.tcb.2016.03.004_bib0535 article-title: Engineering enhanced protein disaggregases for neurodegenerative disease publication-title: Prion doi: 10.1080/19336896.2015.1020277 – volume: 149 start-page: 753 year: 2012 ident: 10.1016/j.tcb.2016.03.004_bib0020 article-title: Cell-free formation of RNA granules: low complexity sequence domains form dynamic fibers within hydrogels publication-title: Cell doi: 10.1016/j.cell.2012.04.017 – volume: 95 start-page: 2748 year: 2000 ident: 10.1016/j.tcb.2016.03.004_bib0350 article-title: Role of SUMO-1-modified PML in nuclear body formation publication-title: Blood doi: 10.1182/blood.V95.9.2748.009k31a_2748_2752 – volume: 324 start-page: 1729 year: 2009 ident: 10.1016/j.tcb.2016.03.004_bib0005 article-title: Germline P granules are liquid droplets that localize by controlled dissolution/condensation publication-title: Science doi: 10.1126/science.1172046 – volume: 6 start-page: 8088 year: 2015 ident: 10.1016/j.tcb.2016.03.004_bib0135 article-title: Liquid demixing of intrinsically disordered proteins is seeded by poly(ADP-ribose) publication-title: Nat. Commun. doi: 10.1038/ncomms9088 – volume: 146 start-page: w14287 year: 2016 ident: 10.1016/j.tcb.2016.03.004_bib0530 article-title: Amyloid-beta pathology and cerebral amyloid angiopathy are frequent in iatrogenic Creutzfeldt–Jakob disease after dural grafting publication-title: Swiss Med. Wkly – volume: 6 start-page: 193 year: 2011 ident: 10.1016/j.tcb.2016.03.004_bib0425 article-title: Parkinson's disease: genetics and pathogenesis publication-title: Annu. Rev. Pathol. doi: 10.1146/annurev-pathol-011110-130242 – volume: 15 start-page: 829 year: 2014 ident: 10.1016/j.tcb.2016.03.004_bib0345 article-title: A census of human RNA-binding proteins publication-title: Nat. Rev. Genet. doi: 10.1038/nrg3813 – volume: 163 start-page: 108 year: 2015 ident: 10.1016/j.tcb.2016.03.004_bib0295 article-title: Phase transition of spindle-associated protein regulate spindle apparatus assembly publication-title: Cell doi: 10.1016/j.cell.2015.08.010 – volume: 11 start-page: 301 year: 2010 ident: 10.1016/j.tcb.2016.03.004_bib0420 article-title: Prion-like transmission of protein aggregates in neurodegenerative diseases publication-title: Nat. Rev. Mol. Cell Biol. doi: 10.1038/nrm2873 – volume: 108 start-page: 20881 year: 2011 ident: 10.1016/j.tcb.2016.03.004_bib0215 article-title: A yeast functional screen predicts new candidate ALS disease genes publication-title: Proc. Natl. Acad. Sci. U.S.A. doi: 10.1073/pnas.1109434108 – volume: 43 start-page: 7535 year: 2015 ident: 10.1016/j.tcb.2016.03.004_bib0250 article-title: Nucleic acid-binding specificity of human FUS protein publication-title: Nucleic Acids Res. doi: 10.1093/nar/gkv679 – volume: 337 start-page: 1047 year: 2012 ident: 10.1016/j.tcb.2016.03.004_bib0025 article-title: Cell biology. Beyond oil and water – phase transitions in cells publication-title: Science doi: 10.1126/science.1223728 – volume: 137 start-page: 146 year: 2009 ident: 10.1016/j.tcb.2016.03.004_bib0070 article-title: A systematic survey identifies prions and illuminates sequence features of prionogenic proteins publication-title: Cell doi: 10.1016/j.cell.2009.02.044 – volume: 21 start-page: 1259 year: 2011 ident: 10.1016/j.tcb.2016.03.004_bib0300 article-title: Limiting amounts of centrosome material set centrosome size in C. elegans embryos publication-title: Curr. Biol. doi: 10.1016/j.cub.2011.06.002 – volume: 84 start-page: 227 year: 2015 ident: 10.1016/j.tcb.2016.03.004_bib0270 article-title: Nuclear ADP-ribosylation and its role in chromatin plasticity, cell differentiation, and epigenetics publication-title: Annu. Rev. Biochem. doi: 10.1146/annurev-biochem-060614-034506 – volume: 34 start-page: 23 year: 2015 ident: 10.1016/j.tcb.2016.03.004_bib0040 article-title: Nuclear bodies: the emerging biophysics of nucleoplasmic phases publication-title: Curr. Opin. Cell Biol. doi: 10.1016/j.ceb.2015.04.003 – volume: 154 start-page: 727 year: 2013 ident: 10.1016/j.tcb.2016.03.004_bib0060 article-title: Altered ribostasis: RNA–protein granules in degenerative disorders publication-title: Cell doi: 10.1016/j.cell.2013.07.038 – volume: 9 start-page: 944 year: 2014 ident: 10.1016/j.tcb.2016.03.004_bib0110 article-title: Granules harboring translationally active mRNAs provide a platform for P-body formation following stress publication-title: Cell Rep. doi: 10.1016/j.celrep.2014.09.040 – volume: 204 start-page: 351 year: 2011 ident: 10.1016/j.tcb.2016.03.004_bib0200 article-title: Promiscuous partnerships in Ewing's sarcoma publication-title: Cancer Genet. doi: 10.1016/j.cancergen.2011.07.008 – volume: 164 start-page: 487 year: 2016 ident: 10.1016/j.tcb.2016.03.004_bib0370 article-title: ATPase-modulated stress granules contain a diverse proteome and substructure publication-title: Cell doi: 10.1016/j.cell.2015.12.038 – volume: 11 start-page: 899 year: 2015 ident: 10.1016/j.tcb.2016.03.004_bib0245 article-title: Polymer physics of intracellular phase transitions publication-title: Nat. Phys. doi: 10.1038/nphys3532 – volume: 2 start-page: a000711 year: 2010 ident: 10.1016/j.tcb.2016.03.004_bib0185 article-title: Biogenesis of nuclear bodies publication-title: Cold Spring Harb. Perspect. Biol. doi: 10.1101/cshperspect.a000711 – volume: 58 start-page: 959 year: 2015 ident: 10.1016/j.tcb.2016.03.004_bib0275 article-title: RNA regulation by poly(ADP-ribose) polymerases publication-title: Mol. Cell doi: 10.1016/j.molcel.2015.01.037 – volume: 14 start-page: 248 year: 2013 ident: 10.1016/j.tcb.2016.03.004_bib0430 article-title: The changing scene of amyotrophic lateral sclerosis publication-title: Nat. Rev. Neurosci. doi: 10.1038/nrn3430 – volume: 5 start-page: 781 year: 2013 ident: 10.1016/j.tcb.2016.03.004_bib0470 article-title: Widespread aggregation and neurodegenerative diseases are associated with supersaturated proteins publication-title: Cell Rep. doi: 10.1016/j.celrep.2013.09.043 – volume: 75 start-page: S51 issue: Suppl. 1 year: 2014 ident: 10.1016/j.tcb.2016.03.004_bib0485 article-title: Oxidative stress affects FET proteins localization and alternative pre-mRNA processing in cellular models of ALS publication-title: Free Radic. Biol. Med. doi: 10.1016/j.freeradbiomed.2014.10.820 – volume: 203 start-page: 875 year: 2013 ident: 10.1016/j.tcb.2016.03.004_bib0115 article-title: Phase transitions and size scaling of membrane-less organelles publication-title: J. Cell Biol. doi: 10.1083/jcb.201308087 – volume: 345 start-page: 1139 year: 2014 ident: 10.1016/j.tcb.2016.03.004_bib0495 article-title: Poly-dipeptides encoded by the C9ORF72 repeats bind nucleoli, impede RNA biogenesis, and kill cells publication-title: Science doi: 10.1126/science.1254917 – volume: 519 start-page: 106 year: 2015 ident: 10.1016/j.tcb.2016.03.004_bib0315 article-title: Folding of an intrinsically disordered protein by phosphorylation as a regulatory switch publication-title: Nature doi: 10.1038/nature13999 – volume: 60 start-page: 231 year: 2015 ident: 10.1016/j.tcb.2016.03.004_bib0330 article-title: Residue-by-residue view of in vitro FUS granules that bind the C-terminal domain of RNA polymerase II publication-title: Mol. Cell doi: 10.1016/j.molcel.2015.09.006 – year: 2014 ident: 10.1016/j.tcb.2016.03.004_bib0150 article-title: Phase transitions of multivalent proteins can promote clustering of membrane receptors publication-title: Elife doi: 10.7554/eLife.04123 – volume: 35 start-page: 531 year: 2015 ident: 10.1016/j.tcb.2016.03.004_bib0480 article-title: Liquids, fibers, and gels: the many phases of neurodegeneration publication-title: Dev. Cell doi: 10.1016/j.devcel.2015.11.014 – volume: 210 start-page: 527 year: 2015 ident: 10.1016/j.tcb.2016.03.004_bib0105 article-title: Paraspeckles: paragons of functional aggregation publication-title: J. Cell Biol. doi: 10.1083/jcb.201507052 – volume: 205 start-page: 613 year: 2014 ident: 10.1016/j.tcb.2016.03.004_bib0285 article-title: Poly(ADP-ribose): an organizer of cellular architecture publication-title: J. Cell Biol. doi: 10.1083/jcb.201402114 – volume: 163 start-page: 406 year: 2015 ident: 10.1016/j.tcb.2016.03.004_bib0405 article-title: Regulated formation of an amyloid-like translational repressor governs gametogenesis publication-title: Cell doi: 10.1016/j.cell.2015.08.060 – volume: 11 start-page: 214 year: 2015 ident: 10.1016/j.tcb.2016.03.004_bib0395 article-title: Poly-ADP-ribosylation of HMGB1 regulates TNFSF10/TRAIL resistance through autophagy publication-title: Autophagy doi: 10.4161/15548627.2014.994400 – volume: 15 start-page: 749 year: 2014 ident: 10.1016/j.tcb.2016.03.004_bib0260 article-title: The structure, function and evolution of proteins that bind DNA and RNA publication-title: Nat. Rev. Mol. Cell Biol. doi: 10.1038/nrm3884 – volume: 149 start-page: 1188 year: 2012 ident: 10.1016/j.tcb.2016.03.004_bib0030 article-title: Getting RNA and protein in phase publication-title: Cell doi: 10.1016/j.cell.2012.05.022 – volume: 24 start-page: 506 year: 2014 ident: 10.1016/j.tcb.2016.03.004_bib0365 article-title: Proteostasis impairment in protein-misfolding and -aggregation diseases publication-title: Trends Cell Biol. doi: 10.1016/j.tcb.2014.05.003 – year: 2015 ident: 10.1016/j.tcb.2016.03.004_bib0160 article-title: Nup98 FG domains from diverse species spontaneously phase-separate into particles with nuclear pore-like permselectivity publication-title: Elife doi: 10.7554/eLife.04251 – volume: 5 start-page: 16607 year: 2015 ident: 10.1016/j.tcb.2016.03.004_bib0085 article-title: Soft viscoelastic properties of nuclear actin age oocytes due to gravitational creep publication-title: Sci. Rep. doi: 10.1038/srep16607 – volume: 1 start-page: 96 year: 2010 ident: 10.1016/j.tcb.2016.03.004_bib0125 article-title: Dynamic control of Cajal body number during zebrafish embryogenesis publication-title: Nucleus doi: 10.4161/nucl.1.1.10680 – volume: 11 start-page: 862 year: 2015 ident: 10.1016/j.tcb.2016.03.004_bib0385 article-title: Determinants of amyloid fibril degradation by the PDZ protease HTRA1 publication-title: Nat. Chem. Biol. doi: 10.1038/nchembio.1931 – volume: 495 start-page: 467 year: 2013 ident: 10.1016/j.tcb.2016.03.004_bib0450 article-title: Mutations in prion-like domains in hnRNPA2B1 and hnRNPA1 cause multisystem proteinopathy and ALS publication-title: Nature doi: 10.1038/nature11922 – volume: 84 start-page: 355 year: 2015 ident: 10.1016/j.tcb.2016.03.004_bib0195 article-title: Biochemical properties and biological functions of FET proteins publication-title: Annu. Rev. Biochem. doi: 10.1146/annurev-biochem-060614-034325 – volume: 44 start-page: 993 year: 2016 ident: 10.1016/j.tcb.2016.03.004_bib0140 article-title: Readers of poly(ADP-ribose): designed to be fit for purpose publication-title: Nucleic Acids Res. doi: 10.1093/nar/gkv1383 – volume: 89 start-page: 1105 year: 2009 ident: 10.1016/j.tcb.2016.03.004_bib0435 article-title: Prions: protein aggregation and infectious diseases publication-title: Physiol. Rev. doi: 10.1152/physrev.00006.2009 – volume: 108 start-page: 4334 year: 2011 ident: 10.1016/j.tcb.2016.03.004_bib0010 article-title: Active liquid-like behavior of nucleoli determines their size and shape in Xenopus laevis oocytes publication-title: Proc. Natl. Acad. Sci. U.S.A. doi: 10.1073/pnas.1017150108 – volume: 150 start-page: 738 year: 2012 ident: 10.1016/j.tcb.2016.03.004_bib0155 article-title: The permeability of reconstituted nuclear pores provides direct evidence for the selective phase model publication-title: Cell doi: 10.1016/j.cell.2012.07.019 – volume: 33 start-page: 2 year: 2008 ident: 10.1016/j.tcb.2016.03.004_bib0165 article-title: Fuzzy complexes: polymorphism and structural disorder in protein–protein interactions publication-title: Trends Biochem. Sci. doi: 10.1016/j.tibs.2007.10.003 – volume: 26 start-page: 40 year: 2016 ident: 10.1016/j.tcb.2016.03.004_bib0515 article-title: Cell biology of prions and prionoids: a status report publication-title: Trends Cell Biol. doi: 10.1016/j.tcb.2015.08.007 – volume: 160 start-page: 798 year: 2015 ident: 10.1016/j.tcb.2016.03.004_bib0445 article-title: SnapShot: genetics of ALS and FTD publication-title: Cell doi: 10.1016/j.cell.2015.01.052 – volume: 10 start-page: 337 year: 2014 ident: 10.1016/j.tcb.2016.03.004_bib0210 article-title: The role of FUS gene variants in neurodegenerative diseases publication-title: Nat. Rev. Neurol. doi: 10.1038/nrneurol.2014.78 – volume: 14 start-page: 617 year: 2013 ident: 10.1016/j.tcb.2016.03.004_bib0375 article-title: Protein rescue from aggregates by powerful molecular chaperone machines publication-title: Nat. Rev. Mol. Cell Biol. doi: 10.1038/nrm3660 – volume: 163 start-page: 829 year: 2015 ident: 10.1016/j.tcb.2016.03.004_bib0410 article-title: The LC domain of hnRNPA2 adopts similar conformations in hydrogel polymers, liquid-like droplets, and nuclei publication-title: Cell doi: 10.1016/j.cell.2015.10.040 – volume: 21 start-page: 14 year: 2011 ident: 10.1016/j.tcb.2016.03.004_bib0120 article-title: Beyond stereospecificity: liquids and mesoscale organization of cytoplasm publication-title: Dev. Cell doi: 10.1016/j.devcel.2011.06.013 – volume: 15 start-page: 1253 year: 2013 ident: 10.1016/j.tcb.2016.03.004_bib0080 article-title: A nuclear F-actin scaffold stabilizes ribonucleoprotein droplets against gravity in large cells publication-title: Nat. Cell Biol. doi: 10.1038/ncb2830 – volume: 152 start-page: 791 year: 2013 ident: 10.1016/j.tcb.2016.03.004_bib0095 article-title: Dual specificity kinase DYRK3 couples stress granule condensation/dissolution to mTORC1 signaling publication-title: Cell doi: 10.1016/j.cell.2013.01.033 – volume: 13 start-page: 167 year: 2011 ident: 10.1016/j.tcb.2016.03.004_bib0180 article-title: Nucleation of nuclear bodies by RNA publication-title: Nat. Cell Biol. doi: 10.1038/ncb2157 – volume: 79 start-page: 416 year: 2013 ident: 10.1016/j.tcb.2016.03.004_bib0460 article-title: Converging mechanisms in ALS and FTD: disrupted RNA and protein homeostasis publication-title: Neuron doi: 10.1016/j.neuron.2013.07.033 – volume: 29 start-page: 90 year: 2016 ident: 10.1016/j.tcb.2016.03.004_bib0540 article-title: A designed inhibitor of p53 aggregation rescues p53 tumor suppression in ovarian carcinomas publication-title: Cancer Cell doi: 10.1016/j.ccell.2015.12.002 – volume: 42 start-page: 307 year: 2014 ident: 10.1016/j.tcb.2016.03.004_bib0500 article-title: PARP-1 dependent recruitment of the amyotrophic lateral sclerosis-associated protein FUS/TLS to sites of oxidative DNA damage publication-title: Nucleic Acids Res. doi: 10.1093/nar/gkt835 – volume: 2011 start-page: 837474 year: 2011 ident: 10.1016/j.tcb.2016.03.004_bib0205 article-title: Dr Jekyll and Mr Hyde: the two faces of the FUS/EWS/TAF15 protein family publication-title: Sarcoma doi: 10.1155/2011/837474 – volume: 112 start-page: E5237 year: 2015 ident: 10.1016/j.tcb.2016.03.004_bib0225 article-title: RNA transcription modulates phase transition-driven nuclear body assembly publication-title: Proc. Natl. Acad. Sci. U.S.A. doi: 10.1073/pnas.1509317112 – volume: 163 start-page: 123 year: 2015 ident: 10.1016/j.tcb.2016.03.004_bib0090 article-title: Phase separation by low complexity domains promotes stress granule assembly and drives pathological fibrillization publication-title: Cell doi: 10.1016/j.cell.2015.09.015 – volume: 58 start-page: 902 year: 2015 ident: 10.1016/j.tcb.2016.03.004_bib0265 article-title: PARPs and ADP-ribosylation: 50 years..and counting publication-title: Mol. Cell doi: 10.1016/j.molcel.2015.06.006 – volume: 13 start-page: 425 year: 2012 ident: 10.1016/j.tcb.2016.03.004_bib0290 article-title: Towards a molecular architecture of centriole assembly publication-title: Nat. Rev. Mol. Cell Biol. doi: 10.1038/nrm3373 – volume: 210 start-page: 529 year: 2015 ident: 10.1016/j.tcb.2016.03.004_bib0100 article-title: Prion-like domains in RNA binding proteins are essential for building subnuclear paraspeckles publication-title: J. Cell Biol. doi: 10.1083/jcb.201504117 – volume: 155 start-page: 1049 year: 2013 ident: 10.1016/j.tcb.2016.03.004_bib0325 article-title: Phosphorylation-regulated binding of RNA polymerase II to fibrous polymers of low-complexity domains publication-title: Cell doi: 10.1016/j.cell.2013.10.033 – volume: 161 start-page: 919 year: 2015 ident: 10.1016/j.tcb.2016.03.004_bib0415 article-title: Widespread proteome remodeling and aggregation in aging C. elegans publication-title: Cell doi: 10.1016/j.cell.2015.03.032 – volume: 60 start-page: 208 year: 2015 ident: 10.1016/j.tcb.2016.03.004_bib0220 article-title: Formation and maturation of phase-separated liquid droplets by RNA-binding proteins publication-title: Mol. Cell doi: 10.1016/j.molcel.2015.08.018 – volume: 60 start-page: 220 year: 2015 ident: 10.1016/j.tcb.2016.03.004_bib0305 article-title: RNA controls polyQ protein phase transitions publication-title: Mol. Cell doi: 10.1016/j.molcel.2015.09.017 – volume: 25 start-page: 641 year: 2015 ident: 10.1016/j.tcb.2016.03.004_bib0170 article-title: Inverse size scaling of the nucleolus by a concentration-dependent phase transition publication-title: Curr. Biol. doi: 10.1016/j.cub.2015.01.012 – volume: 28 start-page: 220 year: 2014 ident: 10.1016/j.tcb.2016.03.004_bib0230 article-title: Construction of synthetic nucleoli in human cells reveals how a major functional nuclear domain is formed and propagated through cell division publication-title: Genes Dev. doi: 10.1101/gad.234591.113 – volume: 11 start-page: 1694 year: 2015 ident: 10.1016/j.tcb.2016.03.004_bib0355 article-title: SUMOylation is an inhibitory constraint that regulates the prion-like aggregation and activity of CPEB3 publication-title: Cell Rep. doi: 10.1016/j.celrep.2015.04.061 – volume: 30 start-page: 39 year: 2014 ident: 10.1016/j.tcb.2016.03.004_bib0035 article-title: Liquid–liquid phase separation in biology publication-title: Annu. Rev. Cell Dev. Biol. doi: 10.1146/annurev-cellbio-100913-013325 – volume: 4 start-page: e06807 year: 2015 ident: 10.1016/j.tcb.2016.03.004_bib0390 article-title: Promiscuous interactions and protein disaggregases determine the material state of stress-inducible RNP granules publication-title: Elife doi: 10.7554/eLife.06807 – volume: 162 start-page: 1286 year: 2015 ident: 10.1016/j.tcb.2016.03.004_bib0400 article-title: Reversible, specific, active aggregates of endogenous proteins assemble upon heat stress publication-title: Cell doi: 10.1016/j.cell.2015.08.041 – volume: 201 start-page: 361 year: 2013 ident: 10.1016/j.tcb.2016.03.004_bib0075 article-title: Stress granules as crucibles of ALS pathogenesis publication-title: J. Cell Biol. doi: 10.1083/jcb.201302044 – volume: 149 start-page: 768 year: 2012 ident: 10.1016/j.tcb.2016.03.004_bib0015 article-title: Cell-free formation of RNA granules: bound RNAs identify features and components of cellular assemblies publication-title: Cell doi: 10.1016/j.cell.2012.04.016
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SubjectTerms	Animals Cell Compartmentation Disease Eukaryotic Cells - metabolism Humans intrinsically disordered proteins liquid demixing low-complexity domains neurodegeneration Pathology Phase Transition protein assembly and aggregation Proteins - metabolism
Title	Phase Separation: Linking Cellular Compartmentalization to Disease
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