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SNARE zippering
SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins are a highly conserved set of membrane-associated proteins that mediate intracellular membrane fusion. Cognate SNAREs from two separate membranes zipper to facilitate membrane apposition and fusion. Though the sta...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Portland Press Ltd.
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4859083/ https://www.ncbi.nlm.nih.gov/pubmed/27154457 http://dx.doi.org/10.1042/BSR20160004 |
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author | Lou, Xiaochu Shin, Yeon-Kyun |
author_facet | Lou, Xiaochu Shin, Yeon-Kyun |
author_sort | Lou, Xiaochu |
collection | PubMed |
description | SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins are a highly conserved set of membrane-associated proteins that mediate intracellular membrane fusion. Cognate SNAREs from two separate membranes zipper to facilitate membrane apposition and fusion. Though the stable post-fusion conformation of SNARE complex has been extensively studied with biochemical and biophysical means, the pathway of SNARE zippering has been elusive. In this review, we describe some recent progress in understanding the pathway of SNARE zippering. We particularly focus on the half-zippered intermediate, which is most likely to serve as the main point of regulation by the auxiliary factors. |
format | Online Article Text |
id | pubmed-4859083 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | Portland Press Ltd. |
record_format | MEDLINE/PubMed |
spelling | pubmed-48590832016-06-01 SNARE zippering Lou, Xiaochu Shin, Yeon-Kyun Biosci Rep Review Articles SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins are a highly conserved set of membrane-associated proteins that mediate intracellular membrane fusion. Cognate SNAREs from two separate membranes zipper to facilitate membrane apposition and fusion. Though the stable post-fusion conformation of SNARE complex has been extensively studied with biochemical and biophysical means, the pathway of SNARE zippering has been elusive. In this review, we describe some recent progress in understanding the pathway of SNARE zippering. We particularly focus on the half-zippered intermediate, which is most likely to serve as the main point of regulation by the auxiliary factors. Portland Press Ltd. 2016-05-06 /pmc/articles/PMC4859083/ /pubmed/27154457 http://dx.doi.org/10.1042/BSR20160004 Text en © 2016 The Author(s) http://creativecommons.org/licenses/by/4.0/ This is an open access article published by Portland Press Limited on behalf of the Biochemical Society and distributed under the Creative Commons Attribution Licence 4.0 (CC BY) (http://creativecommons.org/licenses/by/4.0/) . |
spellingShingle | Review Articles Lou, Xiaochu Shin, Yeon-Kyun SNARE zippering |
title | SNARE zippering |
title_full | SNARE zippering |
title_fullStr | SNARE zippering |
title_full_unstemmed | SNARE zippering |
title_short | SNARE zippering |
title_sort | snare zippering |
topic | Review Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4859083/ https://www.ncbi.nlm.nih.gov/pubmed/27154457 http://dx.doi.org/10.1042/BSR20160004 |
work_keys_str_mv | AT louxiaochu snarezippering AT shinyeonkyun snarezippering |