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Regulation of exocytosis by the exocyst subunit Sec6 and the SM protein Sec1

Trafficking of protein and lipid cargo through the secretory pathway in eukaryotic cells is mediated by membrane-bound vesicles. Secretory vesicle targeting and fusion require a conserved multisubunit protein complex termed the exocyst, which has been implicated in specific tethering of vesicles to...

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Autores principales: Morgera, Francesca, Sallah, Margaret R., Dubuke, Michelle L., Gandhi, Pallavi, Brewer, Daniel N., Carr, Chavela M., Munson, Mary
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The American Society for Cell Biology 2012
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3258177/
https://www.ncbi.nlm.nih.gov/pubmed/22114349
http://dx.doi.org/10.1091/mbc.E11-08-0670
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author Morgera, Francesca
Sallah, Margaret R.
Dubuke, Michelle L.
Gandhi, Pallavi
Brewer, Daniel N.
Carr, Chavela M.
Munson, Mary
author_facet Morgera, Francesca
Sallah, Margaret R.
Dubuke, Michelle L.
Gandhi, Pallavi
Brewer, Daniel N.
Carr, Chavela M.
Munson, Mary
author_sort Morgera, Francesca
collection PubMed
description Trafficking of protein and lipid cargo through the secretory pathway in eukaryotic cells is mediated by membrane-bound vesicles. Secretory vesicle targeting and fusion require a conserved multisubunit protein complex termed the exocyst, which has been implicated in specific tethering of vesicles to sites of polarized exocytosis. The exocyst is directly involved in regulating soluble N-ethylmaleimide–sensitive factor (NSF) attachment protein receptor (SNARE) complexes and membrane fusion through interactions between the Sec6 subunit and the plasma membrane SNARE protein Sec9. Here we show another facet of Sec6 function—it directly binds Sec1, another SNARE regulator, but of the Sec1/Munc18 family. The Sec6–Sec1 interaction is exclusive of Sec6–Sec9 but compatible with Sec6–exocyst assembly. In contrast, the Sec6–exocyst interaction is incompatible with Sec6–Sec9. Therefore, upon vesicle arrival, Sec6 is proposed to release Sec9 in favor of Sec6–exocyst assembly and to simultaneously recruit Sec1 to sites of secretion for coordinated SNARE complex formation and membrane fusion.
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spelling pubmed-32581772012-03-30 Regulation of exocytosis by the exocyst subunit Sec6 and the SM protein Sec1 Morgera, Francesca Sallah, Margaret R. Dubuke, Michelle L. Gandhi, Pallavi Brewer, Daniel N. Carr, Chavela M. Munson, Mary Mol Biol Cell Articles Trafficking of protein and lipid cargo through the secretory pathway in eukaryotic cells is mediated by membrane-bound vesicles. Secretory vesicle targeting and fusion require a conserved multisubunit protein complex termed the exocyst, which has been implicated in specific tethering of vesicles to sites of polarized exocytosis. The exocyst is directly involved in regulating soluble N-ethylmaleimide–sensitive factor (NSF) attachment protein receptor (SNARE) complexes and membrane fusion through interactions between the Sec6 subunit and the plasma membrane SNARE protein Sec9. Here we show another facet of Sec6 function—it directly binds Sec1, another SNARE regulator, but of the Sec1/Munc18 family. The Sec6–Sec1 interaction is exclusive of Sec6–Sec9 but compatible with Sec6–exocyst assembly. In contrast, the Sec6–exocyst interaction is incompatible with Sec6–Sec9. Therefore, upon vesicle arrival, Sec6 is proposed to release Sec9 in favor of Sec6–exocyst assembly and to simultaneously recruit Sec1 to sites of secretion for coordinated SNARE complex formation and membrane fusion. The American Society for Cell Biology 2012-01-15 /pmc/articles/PMC3258177/ /pubmed/22114349 http://dx.doi.org/10.1091/mbc.E11-08-0670 Text en © 2012 Morgera et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0). “ASCB®,” “The American Society for Cell Biology®,” and “Molecular Biology of the Cell®” are registered trademarks of The American Society of Cell Biology.
spellingShingle Articles
Morgera, Francesca
Sallah, Margaret R.
Dubuke, Michelle L.
Gandhi, Pallavi
Brewer, Daniel N.
Carr, Chavela M.
Munson, Mary
Regulation of exocytosis by the exocyst subunit Sec6 and the SM protein Sec1
title Regulation of exocytosis by the exocyst subunit Sec6 and the SM protein Sec1
title_full Regulation of exocytosis by the exocyst subunit Sec6 and the SM protein Sec1
title_fullStr Regulation of exocytosis by the exocyst subunit Sec6 and the SM protein Sec1
title_full_unstemmed Regulation of exocytosis by the exocyst subunit Sec6 and the SM protein Sec1
title_short Regulation of exocytosis by the exocyst subunit Sec6 and the SM protein Sec1
title_sort regulation of exocytosis by the exocyst subunit sec6 and the sm protein sec1
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3258177/
https://www.ncbi.nlm.nih.gov/pubmed/22114349
http://dx.doi.org/10.1091/mbc.E11-08-0670
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