The Intrinsically Disordered Protein Atg13 Mediates Supramolecular Assembly of Autophagy Initiation Complexes
Autophagosome formation in yeast entails starvation-induced assembly of the pre-autophagosomal structure (PAS), in which multiple Atg1 complexes (composed of Atg1, Atg13, and the Atg17-Atg29-Atg31 subcomplex) are initially engaged. However, the molecular mechanisms underlying the multimeric assembly...
Uložené v:
| Vydané v: | Developmental cell Ročník 38; číslo 1; s. 86 - 99 |
|---|---|
| Hlavní autori: | , , , , , , , , , , |
| Médium: | Journal Article |
| Jazyk: | English |
| Vydavateľské údaje: |
United States
11.07.2016
|
| Predmet: | |
| ISSN: | 1878-1551 |
| On-line prístup: | Zistit podrobnosti o prístupe |
| Tagy: |
Pridať tag
Žiadne tagy, Buďte prvý, kto otaguje tento záznam!
|
| Abstract | Autophagosome formation in yeast entails starvation-induced assembly of the pre-autophagosomal structure (PAS), in which multiple Atg1 complexes (composed of Atg1, Atg13, and the Atg17-Atg29-Atg31 subcomplex) are initially engaged. However, the molecular mechanisms underlying the multimeric assembly of these complexes remain unclear. Using structural and biological techniques, we herein demonstrate that Atg13 has a large intrinsically disordered region (IDR) and interacts with two distinct Atg17 molecules using two binding regions in the IDR. We further reveal that these two binding regions are essential not only for Atg1 complex assembly in vitro, but also for PAS organization in vivo. These findings underscore the structural and functional significance of the IDR of Atg13 in autophagy initiation: Atg13 provides intercomplex linkages between Atg17-Atg29-Atg31 complexes, thereby leading to supramolecular self-assembly of Atg1 complexes, in turn accelerating the initial events of autophagy, including autophosphorylation of Atg1, recruitment of Atg9 vesicles, and phosphorylation of Atg9 by Atg1. |
|---|---|
| AbstractList | Autophagosome formation in yeast entails starvation-induced assembly of the pre-autophagosomal structure (PAS), in which multiple Atg1 complexes (composed of Atg1, Atg13, and the Atg17-Atg29-Atg31 subcomplex) are initially engaged. However, the molecular mechanisms underlying the multimeric assembly of these complexes remain unclear. Using structural and biological techniques, we herein demonstrate that Atg13 has a large intrinsically disordered region (IDR) and interacts with two distinct Atg17 molecules using two binding regions in the IDR. We further reveal that these two binding regions are essential not only for Atg1 complex assembly in vitro, but also for PAS organization in vivo. These findings underscore the structural and functional significance of the IDR of Atg13 in autophagy initiation: Atg13 provides intercomplex linkages between Atg17-Atg29-Atg31 complexes, thereby leading to supramolecular self-assembly of Atg1 complexes, in turn accelerating the initial events of autophagy, including autophosphorylation of Atg1, recruitment of Atg9 vesicles, and phosphorylation of Atg9 by Atg1. Autophagosome formation in yeast entails starvation-induced assembly of the pre-autophagosomal structure (PAS), in which multiple Atg1 complexes (composed of Atg1, Atg13, and the Atg17-Atg29-Atg31 subcomplex) are initially engaged. However, the molecular mechanisms underlying the multimeric assembly of these complexes remain unclear. Using structural and biological techniques, we herein demonstrate that Atg13 has a large intrinsically disordered region (IDR) and interacts with two distinct Atg17 molecules using two binding regions in the IDR. We further reveal that these two binding regions are essential not only for Atg1 complex assembly in vitro, but also for PAS organization in vivo. These findings underscore the structural and functional significance of the IDR of Atg13 in autophagy initiation: Atg13 provides intercomplex linkages between Atg17-Atg29-Atg31 complexes, thereby leading to supramolecular self-assembly of Atg1 complexes, in turn accelerating the initial events of autophagy, including autophosphorylation of Atg1, recruitment of Atg9 vesicles, and phosphorylation of Atg9 by Atg1. |
| Author | Ohsumi, Yoshinori Ando, Toshio Fujioka, Yuko Noshiro, Daisuke Noda, Nobuo N Suzuki, Hironori Hirano, Hisashi Suzuki, Sho W Yamamoto, Hayashi Kondo-Kakuta, Chika Kimura, Yayoi |
| Author_xml | – sequence: 1 givenname: Hayashi surname: Yamamoto fullname: Yamamoto, Hayashi organization: Frontier Research Center, Tokyo Institute of Technology, Yokohama 226-8503, Japan – sequence: 2 givenname: Yuko surname: Fujioka fullname: Fujioka, Yuko organization: Institute of Microbial Chemistry (BIKAKEN), Tokyo 141-0021, Japan – sequence: 3 givenname: Sho W surname: Suzuki fullname: Suzuki, Sho W organization: Frontier Research Center, Tokyo Institute of Technology, Yokohama 226-8503, Japan – sequence: 4 givenname: Daisuke surname: Noshiro fullname: Noshiro, Daisuke organization: Department of Physics, College of Science and Engineering, Kanazawa University, Kanazawa 920-1192, Japan – sequence: 5 givenname: Hironori surname: Suzuki fullname: Suzuki, Hironori organization: Institute of Microbial Chemistry (BIKAKEN), Tokyo 141-0021, Japan – sequence: 6 givenname: Chika surname: Kondo-Kakuta fullname: Kondo-Kakuta, Chika organization: Frontier Research Center, Tokyo Institute of Technology, Yokohama 226-8503, Japan – sequence: 7 givenname: Yayoi surname: Kimura fullname: Kimura, Yayoi organization: Advanced Medical Research Center, Yokohama City University, Yokohama 236-0004, Japan – sequence: 8 givenname: Hisashi surname: Hirano fullname: Hirano, Hisashi organization: Advanced Medical Research Center, Yokohama City University, Yokohama 236-0004, Japan – sequence: 9 givenname: Toshio surname: Ando fullname: Ando, Toshio organization: Department of Physics, College of Science and Engineering, Kanazawa University, Kanazawa 920-1192, Japan – sequence: 10 givenname: Nobuo N surname: Noda fullname: Noda, Nobuo N email: nn@bikaken.or.jp organization: Institute of Microbial Chemistry (BIKAKEN), Tokyo 141-0021, Japan. Electronic address: nn@bikaken.or.jp – sequence: 11 givenname: Yoshinori surname: Ohsumi fullname: Ohsumi, Yoshinori email: yohsumi@iri.titech.ac.jp organization: Frontier Research Center, Tokyo Institute of Technology, Yokohama 226-8503, Japan. Electronic address: yohsumi@iri.titech.ac.jp |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/27404361$$D View this record in MEDLINE/PubMed |
| BookMark | eNo1kFtLxDAQhYMo7kX_gUgefWlN0qZNH8t6W1hRcH0uaTPZzdI2NWnF_fcGXGFgGOabw5mzQOe97QGhG0piSmh2f4gVfDfQxixMMQlF-RmaU5GLiHJOZ2jh_YGEJRXkEs1YnpI0yegcdds94HU_OtN708i2PeIH461T4EDhd2dHMD0uxx1N8CsoI0fw-GManOxsC83USodL76Grw6XVuJxGO-zl7hhEzRhwY3u8st3Qwg_4K3ShZevh-tSX6PPpcbt6iTZvz-tVuYkaTvgYSSqErlNeSKoJ5ImuG0ZkrXmi6iQL1pnSQjOZkowWQABA5TotwruUJ8AoW6K7P93B2a8J_Fh1xod8WtmDnXwVUkhpITJRBPT2hE51B6oanOmkO1b_EbFf4wVrtg |
| CitedBy_id | crossref_primary_10_1016_j_drup_2024_101170 crossref_primary_10_1016_j_jmb_2025_168954 crossref_primary_10_1038_s41580_020_0241_0 crossref_primary_10_1083_jcb_202004062 crossref_primary_10_1038_s41568_022_00444_7 crossref_primary_10_1016_j_sbi_2016_09_010 crossref_primary_10_1080_15548627_2021_1909407 crossref_primary_10_15252_embr_202357758 crossref_primary_10_3389_fonc_2024_1364070 crossref_primary_10_1093_jb_mvad099 crossref_primary_10_3390_cells6030023 crossref_primary_10_1038_s41422_020_0297_6 crossref_primary_10_1016_j_jmb_2019_07_027 crossref_primary_10_62347_QCPV6064 crossref_primary_10_1016_j_biopha_2020_110065 crossref_primary_10_1038_s41556_024_01572_y crossref_primary_10_1016_j_chemphyslip_2018_11_001 crossref_primary_10_1186_s12929_024_00993_z crossref_primary_10_1016_j_ccell_2020_12_003 crossref_primary_10_1016_j_cell_2024_04_007 crossref_primary_10_7554_eLife_43088 crossref_primary_10_1080_15548627_2023_2259708 crossref_primary_10_1016_j_molcel_2019_03_033 crossref_primary_10_3389_fpls_2020_00565 crossref_primary_10_1038_s41594_024_01217_6 crossref_primary_10_1093_genetics_iyaf007 crossref_primary_10_1002_2211_5463_12355 crossref_primary_10_1091_mbc_E17_04_0258 crossref_primary_10_1016_j_virusres_2017_09_006 crossref_primary_10_1371_journal_pbio_3000718 crossref_primary_10_3390_cells11071086 crossref_primary_10_1007_s41745_016_0015_z crossref_primary_10_3389_fcimb_2021_771010 crossref_primary_10_1080_15548627_2016_1277312 crossref_primary_10_1016_j_psj_2022_101750 crossref_primary_10_1016_j_jmb_2025_169235 crossref_primary_10_3390_cancers12020352 crossref_primary_10_1007_s00018_017_2560_7 crossref_primary_10_1080_15548627_2019_1646540 crossref_primary_10_1083_jcb_202210017 crossref_primary_10_1242_bio_022053 crossref_primary_10_7554_eLife_101531 crossref_primary_10_1002_1873_3468_14741 crossref_primary_10_1002_1873_3468_14742 crossref_primary_10_1007_s00018_022_04468_y crossref_primary_10_1038_s41467_021_27420_3 crossref_primary_10_1080_0194262X_2016_1273814 crossref_primary_10_1111_febs_70112 crossref_primary_10_1091_mbc_E23_12_0470 crossref_primary_10_1016_j_ceb_2024_102393 crossref_primary_10_3390_jof7110903 crossref_primary_10_1146_annurev_biochem_090920_103246 crossref_primary_10_3390_biom9020039 crossref_primary_10_1002_EXP_20240112 crossref_primary_10_1016_j_devcel_2017_03_007 crossref_primary_10_1016_j_ymeth_2022_08_008 crossref_primary_10_7554_eLife_101531_3 crossref_primary_10_1002_ptr_7551 crossref_primary_10_1016_j_bbrc_2016_12_112 crossref_primary_10_1038_s41576_022_00562_w crossref_primary_10_1038_s41556_024_01348_4 crossref_primary_10_1016_j_bbamcr_2021_119064 crossref_primary_10_1016_j_molcel_2024_12_005 crossref_primary_10_1016_j_phrs_2020_104758 crossref_primary_10_3389_fcell_2021_631486 crossref_primary_10_1016_j_bbrc_2025_151468 crossref_primary_10_3389_fimmu_2024_1356369 crossref_primary_10_1016_j_devcel_2020_06_033 crossref_primary_10_1080_15548627_2019_1659615 crossref_primary_10_3389_fpls_2018_01837 crossref_primary_10_2183_pjab_101_005 crossref_primary_10_1016_j_jmb_2025_168964 crossref_primary_10_3390_biom14121517 crossref_primary_10_1038_s41564_022_01314_6 crossref_primary_10_3389_fcell_2022_910640 crossref_primary_10_1016_j_ceb_2020_02_012 crossref_primary_10_1016_j_biochi_2021_12_002 crossref_primary_10_1042_BST20240015 crossref_primary_10_3390_cells8121627 crossref_primary_10_1016_j_sbi_2021_11_014 crossref_primary_10_1016_j_jmb_2017_01_003 crossref_primary_10_1016_j_molcel_2021_10_024 crossref_primary_10_1083_jcb_201710116 crossref_primary_10_1016_j_jmb_2019_09_005 crossref_primary_10_3390_cells10051258 crossref_primary_10_1038_s41586_020_1977_6 crossref_primary_10_1039_D2RA05855C crossref_primary_10_1186_s12943_024_02217_2 crossref_primary_10_1042_BCJ20200849 crossref_primary_10_3390_biom13010015 crossref_primary_10_3389_fonc_2025_1614378 crossref_primary_10_3390_cells10113124 crossref_primary_10_1083_jcb_202310049 crossref_primary_10_1038_s44318_024_00272_5 crossref_primary_10_1080_15548627_2024_2447207 crossref_primary_10_1146_annurev_biochem_061516_044820 crossref_primary_10_1083_jcb_202309057 crossref_primary_10_1007_s00203_023_03683_w crossref_primary_10_3389_fbioe_2022_849768 crossref_primary_10_1093_plcell_koac251 crossref_primary_10_15252_embj_2022113349 crossref_primary_10_1016_j_ceb_2020_12_011 crossref_primary_10_3389_fphar_2023_1287234 crossref_primary_10_1080_15548627_2019_1648117 crossref_primary_10_1038_s41594_025_01678_3 crossref_primary_10_1007_s12551_017_0281_7 crossref_primary_10_1016_j_ejmech_2023_116117 crossref_primary_10_3390_ijms242015036 crossref_primary_10_1080_15548627_2017_1387342 crossref_primary_10_1242_jcs_223792 crossref_primary_10_1007_s00018_022_04393_0 crossref_primary_10_1371_journal_pcbi_1005817 crossref_primary_10_1093_nar_gkaa455 crossref_primary_10_1016_j_molcel_2018_10_040 crossref_primary_10_1083_jcb_202107151 crossref_primary_10_3390_ijms24010148 crossref_primary_10_1016_j_tcb_2025_01_010 crossref_primary_10_1042_BST20200130 crossref_primary_10_1155_2023_8257217 crossref_primary_10_1038_s44319_023_00055_9 crossref_primary_10_1080_15548627_2022_2136340 crossref_primary_10_15252_embr_202051136 crossref_primary_10_1016_j_pbi_2018_09_004 crossref_primary_10_4236_ym_2017_11002 crossref_primary_10_1016_j_tplants_2016_11_015 crossref_primary_10_3390_cells14090636 crossref_primary_10_3390_ph16010092 crossref_primary_10_1002_1873_3468_14717 crossref_primary_10_3390_biomedicines10071596 crossref_primary_10_1016_j_bbrc_2018_09_011 crossref_primary_10_1016_j_bbamcr_2020_118855 crossref_primary_10_1016_j_jmb_2024_168691 crossref_primary_10_1016_j_jplph_2022_153653 crossref_primary_10_1038_s41421_020_0161_3 crossref_primary_10_1002_pro_3623 crossref_primary_10_1080_15548627_2022_2080383 crossref_primary_10_3390_ijms241914887 crossref_primary_10_1016_j_cbpa_2019_05_010 crossref_primary_10_1038_s41565_020_00798_9 crossref_primary_10_3390_biom7030052 crossref_primary_10_1242_jcs_235002 crossref_primary_10_1080_15548627_2020_1776474 crossref_primary_10_1038_s44318_024_00036_1 crossref_primary_10_1080_15548627_2023_2175305 crossref_primary_10_1016_j_molcel_2017_07_003 crossref_primary_10_1631_jzus_B2300402 crossref_primary_10_1016_j_tplants_2018_05_002 crossref_primary_10_1016_j_cellimm_2017_06_004 crossref_primary_10_3390_biom12121876 crossref_primary_10_1080_15548627_2023_2182478 crossref_primary_10_1186_s12943_020_1138_4 crossref_primary_10_1016_j_canlet_2024_216779 crossref_primary_10_1093_jb_mvab017 crossref_primary_10_1038_s41556_021_00669_y crossref_primary_10_7554_eLife_58073 crossref_primary_10_1007_s00018_017_2657_z crossref_primary_10_1074_jbc_M116_762948 crossref_primary_10_3390_cells12040668 crossref_primary_10_1016_j_bbagen_2022_130203 crossref_primary_10_1111_febs_15334 crossref_primary_10_1016_j_jmb_2018_04_007 crossref_primary_10_1242_jcs_253682 crossref_primary_10_1007_s00018_020_03621_9 crossref_primary_10_1177_25152564231162495 crossref_primary_10_3389_fcell_2025_1520850 |
| ContentType | Journal Article |
| Copyright | Copyright © 2016 Elsevier Inc. All rights reserved. |
| Copyright_xml | – notice: Copyright © 2016 Elsevier Inc. All rights reserved. |
| DBID | CGR CUY CVF ECM EIF NPM 7X8 |
| DOI | 10.1016/j.devcel.2016.06.015 |
| DatabaseName | Medline MEDLINE MEDLINE (Ovid) MEDLINE MEDLINE PubMed MEDLINE - Academic |
| DatabaseTitle | MEDLINE Medline Complete MEDLINE with Full Text PubMed MEDLINE (Ovid) MEDLINE - Academic |
| DatabaseTitleList | MEDLINE - Academic MEDLINE |
| Database_xml | – sequence: 1 dbid: NPM name: PubMed url: http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed sourceTypes: Index Database – sequence: 2 dbid: 7X8 name: MEDLINE - Academic url: https://search.proquest.com/medline sourceTypes: Aggregation Database |
| DeliveryMethod | no_fulltext_linktorsrc |
| Discipline | Biology |
| EISSN | 1878-1551 |
| EndPage | 99 |
| ExternalDocumentID | 27404361 |
| Genre | Research Support, Non-U.S. Gov't Journal Article |
| GroupedDBID | --- --K 0R~ 0SF 1~5 2WC 4.4 457 4G. 53G 5GY 62- 6I. 7-5 AACTN AAEDT AAEDW AAFTH AAKRW AALRI AAMRU AAVLU AAXUO ABJNI ABMAC ABVKL ACGFO ACGFS ACNCT ADBBV ADEZE ADVLN AEFWE AENEX AEXQZ AFFNX AFTJW AGKMS AITUG AKAPO AKRWK ALMA_UNASSIGNED_HOLDINGS AMRAJ ASPBG AVWKF AZFZN BAWUL CGR CS3 CUY CVF D0L DIK DU5 E3Z EBS ECM EIF EJD F5P FCP FDB FEDTE FIRID HVGLF IHE IXB J1W JIG M3Z M41 NCXOZ NPM O-L O9- OK1 P2P RCE RIG ROL RPZ SDG SES SSZ TR2 7X8 AAYWO ABDGV ACVFH ADCNI AEUPX AFPUW AIGII AKBMS AKYEP APXCP EFKBS |
| ID | FETCH-LOGICAL-c505t-a188fb459a1f0e73fbc20abf53db364042df8f2a40619e0eeed7f49187153e212 |
| IEDL.DBID | 7X8 |
| ISICitedReferencesCount | 176 |
| ISICitedReferencesURI | http://www.webofscience.com/api/gateway?GWVersion=2&SrcApp=Summon&SrcAuth=ProQuest&DestLinkType=CitingArticles&DestApp=WOS_CPL&KeyUT=000380073400012&url=https%3A%2F%2Fcvtisr.summon.serialssolutions.com%2F%23%21%2Fsearch%3Fho%3Df%26include.ft.matches%3Dt%26l%3Dnull%26q%3D |
| IngestDate | Sun Sep 28 06:08:14 EDT 2025 Thu Jan 02 23:08:19 EST 2025 |
| IsDoiOpenAccess | false |
| IsOpenAccess | true |
| IsPeerReviewed | true |
| IsScholarly | true |
| Issue | 1 |
| Language | English |
| License | Copyright © 2016 Elsevier Inc. All rights reserved. |
| LinkModel | DirectLink |
| MergedId | FETCHMERGED-LOGICAL-c505t-a188fb459a1f0e73fbc20abf53db364042df8f2a40619e0eeed7f49187153e212 |
| Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
| OpenAccessLink | https://dx.doi.org/10.1016/j.devcel.2016.06.015 |
| PMID | 27404361 |
| PQID | 1804198689 |
| PQPubID | 23479 |
| PageCount | 14 |
| ParticipantIDs | proquest_miscellaneous_1804198689 pubmed_primary_27404361 |
| PublicationCentury | 2000 |
| PublicationDate | 2016-07-11 |
| PublicationDateYYYYMMDD | 2016-07-11 |
| PublicationDate_xml | – month: 07 year: 2016 text: 2016-07-11 day: 11 |
| PublicationDecade | 2010 |
| PublicationPlace | United States |
| PublicationPlace_xml | – name: United States |
| PublicationTitle | Developmental cell |
| PublicationTitleAlternate | Dev Cell |
| PublicationYear | 2016 |
| SSID | ssj0016180 |
| Score | 2.583839 |
| Snippet | Autophagosome formation in yeast entails starvation-induced assembly of the pre-autophagosomal structure (PAS), in which multiple Atg1 complexes (composed of... |
| SourceID | proquest pubmed |
| SourceType | Aggregation Database Index Database |
| StartPage | 86 |
| SubjectTerms | Adaptor Proteins, Signal Transducing - chemistry Adaptor Proteins, Signal Transducing - genetics Adaptor Proteins, Signal Transducing - metabolism Amino Acid Sequence Autophagy Autophagy-Related Proteins - chemistry Autophagy-Related Proteins - genetics Autophagy-Related Proteins - metabolism Intrinsically Disordered Proteins - chemistry Intrinsically Disordered Proteins - genetics Intrinsically Disordered Proteins - metabolism Membrane Proteins - chemistry Membrane Proteins - genetics Membrane Proteins - metabolism Multiprotein Complexes - chemistry Multiprotein Complexes - genetics Multiprotein Complexes - metabolism Phagosomes - physiology Phosphorylation Protein Binding Protein Conformation Protein Kinases - chemistry Protein Kinases - genetics Protein Kinases - metabolism Saccharomyces cerevisiae - genetics Saccharomyces cerevisiae - growth & development Saccharomyces cerevisiae - metabolism Saccharomyces cerevisiae Proteins - chemistry Saccharomyces cerevisiae Proteins - genetics Saccharomyces cerevisiae Proteins - metabolism Sequence Homology, Amino Acid |
| Title | The Intrinsically Disordered Protein Atg13 Mediates Supramolecular Assembly of Autophagy Initiation Complexes |
| URI | https://www.ncbi.nlm.nih.gov/pubmed/27404361 https://www.proquest.com/docview/1804198689 |
| Volume | 38 |
| WOSCitedRecordID | wos000380073400012&url=https%3A%2F%2Fcvtisr.summon.serialssolutions.com%2F%23%21%2Fsearch%3Fho%3Df%26include.ft.matches%3Dt%26l%3Dnull%26q%3D |
| hasFullText | |
| inHoldings | 1 |
| isFullTextHit | |
| isPrint | |
| link | http://cvtisr.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwpV1La8MwDDbbusEuez-6Fx7sGhYnceKcRhkrG6ylsAe9FSeWS6BNuiYt67-fnAc9DQa7hFwcgiRLnyT7EyF3TmCrQDFpyUhwy-Pg45sKrUCFERcxBqjyIu3na9Dvi-EwHNQFt7w-Vtn4xNJRqyw2NfJ7ZohyQuGL8GH2ZZmpUaa7Wo_Q2CQtF6GMsepguO4i-LiouS5XnulSsIzBNByYX7J2Mv47sCwDTHf_v792QPZqaEk7lS0ckg1Ij8hONWxydUymaBH0JS3mSVpqZrKiDfUmKDowfA1JSjvFmLm0Vw7wgJy-LWZzOW1G6FLTIp5GuDLTtLMwnARyvMKPJkWlYWrcywS-IT8hH92n98dnqx62YMUIggpLMiF05PFQMm1D4OoodmwZae6qyPU93NtKC-1IAwBCsAFja6C9kGHCxV3AAHhKttIshXNCI3BsXwUeImLhadeREjEp5mEo9phxAW1y28hxhMZsOhQyhWyRj9aSbJOzShmjWcW6McL02dDls4s_rL4ku0bHpgbL2BVpadzKcE2242WR5POb0krw2R_0fgD9xMoQ |
| linkProvider | ProQuest |
| openUrl | ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=The+Intrinsically+Disordered+Protein+Atg13+Mediates+Supramolecular+Assembly+of+Autophagy+Initiation+Complexes&rft.jtitle=Developmental+cell&rft.au=Yamamoto%2C+Hayashi&rft.au=Fujioka%2C+Yuko&rft.au=Suzuki%2C+Sho+W&rft.au=Noshiro%2C+Daisuke&rft.date=2016-07-11&rft.eissn=1878-1551&rft.volume=38&rft.issue=1&rft.spage=86&rft_id=info:doi/10.1016%2Fj.devcel.2016.06.015&rft_id=info%3Apmid%2F27404361&rft_id=info%3Apmid%2F27404361&rft.externalDocID=27404361 |