Rab6 regulates transport and targeting of exocytotic carriers

Constitutive exocytosis delivers newly synthesized proteins, lipids, and other molecules from the Golgi apparatus to the cell surface. This process is mediated by vesicles, which bud off the trans-Golgi network, move along cytoskeletal filaments, and fuse with the plasma membrane. Here, we show that...

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Vydané v:	Developmental cell Ročník 13; číslo 2; s. 305
Hlavní autori:	Grigoriev, Ilya, Splinter, Daniël, Keijzer, Nanda, Wulf, Phebe S, Demmers, Jeroen, Ohtsuka, Toshihisa, Modesti, Mauro, Maly, Ivan V, Grosveld, Frank, Hoogenraad, Casper C, Akhmanova, Anna
Médium:	Journal Article
Jazyk:	English
Vydavateľské údaje:	United States 01.08.2007
Predmet:	Adaptor Proteins, Signal Transducing - metabolism Animals Biological Transport Biomarkers - metabolism Cell Line Cell Membrane - metabolism Cytoplasm - metabolism Dogs Dyneins - metabolism Exocytosis HeLa Cells Humans Kinesin - metabolism Membrane Fusion Nerve Tissue Proteins - metabolism rab GTP-Binding Proteins - metabolism Rats Transport Vesicles - metabolism
ISSN:	1534-5807
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Abstract	Constitutive exocytosis delivers newly synthesized proteins, lipids, and other molecules from the Golgi apparatus to the cell surface. This process is mediated by vesicles, which bud off the trans-Golgi network, move along cytoskeletal filaments, and fuse with the plasma membrane. Here, we show that the small GTPase Rab6 marks exocytotic vesicles and, together with the microtubule plus-end-directed motor kinesin-1, stimulates their processive microtubule-based transport to the cell periphery. Furthermore, Rab6 directs targeting of secretory vesicles to plasma-membrane sites enriched in the cortical protein ELKS, a known Rab6 binding partner. Our data demonstrate that although Rab6 is not essential for secretion, it controls the organization of exocytosis within the cellular space.
AbstractList	Constitutive exocytosis delivers newly synthesized proteins, lipids, and other molecules from the Golgi apparatus to the cell surface. This process is mediated by vesicles, which bud off the trans-Golgi network, move along cytoskeletal filaments, and fuse with the plasma membrane. Here, we show that the small GTPase Rab6 marks exocytotic vesicles and, together with the microtubule plus-end-directed motor kinesin-1, stimulates their processive microtubule-based transport to the cell periphery. Furthermore, Rab6 directs targeting of secretory vesicles to plasma-membrane sites enriched in the cortical protein ELKS, a known Rab6 binding partner. Our data demonstrate that although Rab6 is not essential for secretion, it controls the organization of exocytosis within the cellular space.Constitutive exocytosis delivers newly synthesized proteins, lipids, and other molecules from the Golgi apparatus to the cell surface. This process is mediated by vesicles, which bud off the trans-Golgi network, move along cytoskeletal filaments, and fuse with the plasma membrane. Here, we show that the small GTPase Rab6 marks exocytotic vesicles and, together with the microtubule plus-end-directed motor kinesin-1, stimulates their processive microtubule-based transport to the cell periphery. Furthermore, Rab6 directs targeting of secretory vesicles to plasma-membrane sites enriched in the cortical protein ELKS, a known Rab6 binding partner. Our data demonstrate that although Rab6 is not essential for secretion, it controls the organization of exocytosis within the cellular space. Constitutive exocytosis delivers newly synthesized proteins, lipids, and other molecules from the Golgi apparatus to the cell surface. This process is mediated by vesicles, which bud off the trans-Golgi network, move along cytoskeletal filaments, and fuse with the plasma membrane. Here, we show that the small GTPase Rab6 marks exocytotic vesicles and, together with the microtubule plus-end-directed motor kinesin-1, stimulates their processive microtubule-based transport to the cell periphery. Furthermore, Rab6 directs targeting of secretory vesicles to plasma-membrane sites enriched in the cortical protein ELKS, a known Rab6 binding partner. Our data demonstrate that although Rab6 is not essential for secretion, it controls the organization of exocytosis within the cellular space.
Author	Ohtsuka, Toshihisa Wulf, Phebe S Maly, Ivan V Demmers, Jeroen Grigoriev, Ilya Grosveld, Frank Hoogenraad, Casper C Splinter, Daniël Akhmanova, Anna Modesti, Mauro Keijzer, Nanda
Author_xml	– sequence: 1 givenname: Ilya surname: Grigoriev fullname: Grigoriev, Ilya organization: Department of Cell Biology, Erasmus Medical Center, 3000 CA Rotterdam, The Netherlands – sequence: 2 givenname: Daniël surname: Splinter fullname: Splinter, Daniël – sequence: 3 givenname: Nanda surname: Keijzer fullname: Keijzer, Nanda – sequence: 4 givenname: Phebe S surname: Wulf fullname: Wulf, Phebe S – sequence: 5 givenname: Jeroen surname: Demmers fullname: Demmers, Jeroen – sequence: 6 givenname: Toshihisa surname: Ohtsuka fullname: Ohtsuka, Toshihisa – sequence: 7 givenname: Mauro surname: Modesti fullname: Modesti, Mauro – sequence: 8 givenname: Ivan V surname: Maly fullname: Maly, Ivan V – sequence: 9 givenname: Frank surname: Grosveld fullname: Grosveld, Frank – sequence: 10 givenname: Casper C surname: Hoogenraad fullname: Hoogenraad, Casper C – sequence: 11 givenname: Anna surname: Akhmanova fullname: Akhmanova, Anna
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SubjectTerms	Adaptor Proteins, Signal Transducing - metabolism Animals Biological Transport Biomarkers - metabolism Cell Line Cell Membrane - metabolism Cytoplasm - metabolism Dogs Dyneins - metabolism Exocytosis HeLa Cells Humans Kinesin - metabolism Membrane Fusion Nerve Tissue Proteins - metabolism rab GTP-Binding Proteins - metabolism Rats Transport Vesicles - metabolism
Title	Rab6 regulates transport and targeting of exocytotic carriers
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