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Organization and dynamics of SNARE proteins in the presynaptic membrane

Our view of the lateral organization of lipids and proteins in the plasma membrane has evolved substantially in the last few decades. It is widely accepted that many, if not all, plasma membrane proteins and lipids are organized in specific domains. These domains vary widely in size, composition, an...

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Detalles Bibliográficos
Autores principales: Milovanovic, Dragomir, Jahn, Reinhard
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4365744/
https://www.ncbi.nlm.nih.gov/pubmed/25852575
http://dx.doi.org/10.3389/fphys.2015.00089
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author Milovanovic, Dragomir
Jahn, Reinhard
author_facet Milovanovic, Dragomir
Jahn, Reinhard
author_sort Milovanovic, Dragomir
collection PubMed
description Our view of the lateral organization of lipids and proteins in the plasma membrane has evolved substantially in the last few decades. It is widely accepted that many, if not all, plasma membrane proteins and lipids are organized in specific domains. These domains vary widely in size, composition, and stability, and they represent platforms governing diverse cell functions. The presynaptic plasma membrane is a well-studied example of a membrane which undergoes rearrangements, especially during exo- and endocytosis. Many proteins and lipids involved in presynaptic function are known, and major efforts have been made to understand their spatial organization and dynamics. Here, we focus on the mechanisms underlying the organization of SNAREs, the key proteins of the fusion machinery, in distinct domains, and we discuss the functional significance of these clusters.
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spelling pubmed-43657442015-04-07 Organization and dynamics of SNARE proteins in the presynaptic membrane Milovanovic, Dragomir Jahn, Reinhard Front Physiol Physiology Our view of the lateral organization of lipids and proteins in the plasma membrane has evolved substantially in the last few decades. It is widely accepted that many, if not all, plasma membrane proteins and lipids are organized in specific domains. These domains vary widely in size, composition, and stability, and they represent platforms governing diverse cell functions. The presynaptic plasma membrane is a well-studied example of a membrane which undergoes rearrangements, especially during exo- and endocytosis. Many proteins and lipids involved in presynaptic function are known, and major efforts have been made to understand their spatial organization and dynamics. Here, we focus on the mechanisms underlying the organization of SNAREs, the key proteins of the fusion machinery, in distinct domains, and we discuss the functional significance of these clusters. Frontiers Media S.A. 2015-03-19 /pmc/articles/PMC4365744/ /pubmed/25852575 http://dx.doi.org/10.3389/fphys.2015.00089 Text en Copyright © 2015 Milovanovic and Jahn. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
spellingShingle Physiology
Milovanovic, Dragomir
Jahn, Reinhard
Organization and dynamics of SNARE proteins in the presynaptic membrane
title Organization and dynamics of SNARE proteins in the presynaptic membrane
title_full Organization and dynamics of SNARE proteins in the presynaptic membrane
title_fullStr Organization and dynamics of SNARE proteins in the presynaptic membrane
title_full_unstemmed Organization and dynamics of SNARE proteins in the presynaptic membrane
title_short Organization and dynamics of SNARE proteins in the presynaptic membrane
title_sort organization and dynamics of snare proteins in the presynaptic membrane
topic Physiology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4365744/
https://www.ncbi.nlm.nih.gov/pubmed/25852575
http://dx.doi.org/10.3389/fphys.2015.00089
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