The mesoscale organization of syntaxin 1A and SNAP25 is determined by SNARE–SNARE interactions

SNARE proteins have been described as the effectors of fusion events in the secretory pathway more than two decades ago. The strong interactions between SNARE domains are clearly important in membrane fusion, but it is unclear whether they are involved in any other cellular processes. Here, we analy...

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Autores principales:	Jasmin Mertins, Jérôme Finke, Ricarda Sies, Kerstin M Rink, Jan Hasenauer, Thorsten Lang
Formato:	article
Lenguaje:	EN
Publicado:	eLife Sciences Publications Ltd 2021
Materias:	plasma membrane exocytosis protein-nanoclustering microdomains Medicine R Science Q Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/85d1dbe8e1ba4bbaade4b2a63292a7c7
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spelling	oai:doaj.org-article:85d1dbe8e1ba4bbaade4b2a63292a7c72021-11-29T12:41:11ZThe mesoscale organization of syntaxin 1A and SNAP25 is determined by SNARE–SNARE interactions10.7554/eLife.692362050-084Xe69236https://doaj.org/article/85d1dbe8e1ba4bbaade4b2a63292a7c72021-11-01T00:00:00Zhttps://elifesciences.org/articles/69236https://doaj.org/toc/2050-084XSNARE proteins have been described as the effectors of fusion events in the secretory pathway more than two decades ago. The strong interactions between SNARE domains are clearly important in membrane fusion, but it is unclear whether they are involved in any other cellular processes. Here, we analyzed two classical SNARE proteins, syntaxin 1A and SNAP25. Although they are supposed to be engaged in tight complexes, we surprisingly find them largely segregated in the plasma membrane. Syntaxin 1A only occupies a small fraction of the plasma membrane area. Yet, we find it is able to redistribute the far more abundant SNAP25 on the mesoscale by gathering crowds of SNAP25 molecules onto syntaxin clusters in a SNARE-domain-dependent manner. Our data suggest that SNARE domain interactions are not only involved in driving membrane fusion on the nanoscale, but also play an important role in controlling the general organization of proteins on the mesoscale. Further, we propose these mechanisms preserve active syntaxin 1A–SNAP25 complexes at the plasma membrane.Jasmin MertinsJérôme FinkeRicarda SiesKerstin M RinkJan HasenauerThorsten LangeLife Sciences Publications Ltdarticleplasma membraneexocytosisprotein-nanoclusteringmicrodomainsMedicineRScienceQBiology (General)QH301-705.5ENeLife, Vol 10 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	plasma membrane exocytosis protein-nanoclustering microdomains Medicine R Science Q Biology (General) QH301-705.5
spellingShingle	plasma membrane exocytosis protein-nanoclustering microdomains Medicine R Science Q Biology (General) QH301-705.5 Jasmin Mertins Jérôme Finke Ricarda Sies Kerstin M Rink Jan Hasenauer Thorsten Lang The mesoscale organization of syntaxin 1A and SNAP25 is determined by SNARE–SNARE interactions
description	SNARE proteins have been described as the effectors of fusion events in the secretory pathway more than two decades ago. The strong interactions between SNARE domains are clearly important in membrane fusion, but it is unclear whether they are involved in any other cellular processes. Here, we analyzed two classical SNARE proteins, syntaxin 1A and SNAP25. Although they are supposed to be engaged in tight complexes, we surprisingly find them largely segregated in the plasma membrane. Syntaxin 1A only occupies a small fraction of the plasma membrane area. Yet, we find it is able to redistribute the far more abundant SNAP25 on the mesoscale by gathering crowds of SNAP25 molecules onto syntaxin clusters in a SNARE-domain-dependent manner. Our data suggest that SNARE domain interactions are not only involved in driving membrane fusion on the nanoscale, but also play an important role in controlling the general organization of proteins on the mesoscale. Further, we propose these mechanisms preserve active syntaxin 1A–SNAP25 complexes at the plasma membrane.
format	article
author	Jasmin Mertins Jérôme Finke Ricarda Sies Kerstin M Rink Jan Hasenauer Thorsten Lang
author_facet	Jasmin Mertins Jérôme Finke Ricarda Sies Kerstin M Rink Jan Hasenauer Thorsten Lang
author_sort	Jasmin Mertins
title	The mesoscale organization of syntaxin 1A and SNAP25 is determined by SNARE–SNARE interactions
title_short	The mesoscale organization of syntaxin 1A and SNAP25 is determined by SNARE–SNARE interactions
title_full	The mesoscale organization of syntaxin 1A and SNAP25 is determined by SNARE–SNARE interactions
title_fullStr	The mesoscale organization of syntaxin 1A and SNAP25 is determined by SNARE–SNARE interactions
title_full_unstemmed	The mesoscale organization of syntaxin 1A and SNAP25 is determined by SNARE–SNARE interactions
title_sort	mesoscale organization of syntaxin 1a and snap25 is determined by snare–snare interactions
publisher	eLife Sciences Publications Ltd
publishDate	2021
url	https://doaj.org/article/85d1dbe8e1ba4bbaade4b2a63292a7c7
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The mesoscale organization of syntaxin 1A and SNAP25 is determined by SNARE–SNARE interactions

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