Cargando…
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...
Autores principales: | , , , , , , |
---|---|
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 |
_version_ | 1782221242894385152 |
---|---|
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. |
format | Online Article Text |
id | pubmed-3258177 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2012 |
publisher | The American Society for Cell Biology |
record_format | MEDLINE/PubMed |
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 |
work_keys_str_mv | AT morgerafrancesca regulationofexocytosisbytheexocystsubunitsec6andthesmproteinsec1 AT sallahmargaretr regulationofexocytosisbytheexocystsubunitsec6andthesmproteinsec1 AT dubukemichellel regulationofexocytosisbytheexocystsubunitsec6andthesmproteinsec1 AT gandhipallavi regulationofexocytosisbytheexocystsubunitsec6andthesmproteinsec1 AT brewerdanieln regulationofexocytosisbytheexocystsubunitsec6andthesmproteinsec1 AT carrchavelam regulationofexocytosisbytheexocystsubunitsec6andthesmproteinsec1 AT munsonmary regulationofexocytosisbytheexocystsubunitsec6andthesmproteinsec1 |