Conserved arginine residues in synaptotagmin 1 regulate fusion pore expansion through membrane contact

Synaptotagmin 1 (Syt1) is the calcium sensor for fast synchronous neurotransmitter release but the mechanism by which it functions is still under debate. Here, the authors combine EPR measurements and functional studies and observe that different faces of the Syt1 C2B domain play different roles in...

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Autores principales:	Sarah B. Nyenhuis, Nakul Karandikar, Volker Kiessling, Alex J. B. Kreutzberger, Anusa Thapa, Binyong Liang, Lukas K. Tamm, David S. Cafiso
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/81777fc5abd14f21a6ee0ae5308e9f0f
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spelling	oai:doaj.org-article:81777fc5abd14f21a6ee0ae5308e9f0f2021-12-02T14:06:16ZConserved arginine residues in synaptotagmin 1 regulate fusion pore expansion through membrane contact10.1038/s41467-021-21090-x2041-1723https://doaj.org/article/81777fc5abd14f21a6ee0ae5308e9f0f2021-02-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-21090-xhttps://doaj.org/toc/2041-1723Synaptotagmin 1 (Syt1) is the calcium sensor for fast synchronous neurotransmitter release but the mechanism by which it functions is still under debate. Here, the authors combine EPR measurements and functional studies and observe that different faces of the Syt1 C2B domain play different roles in regulating neurotransmitter release and they show that the expansion of the fusion pore is mediated by membrane contact of the C2B arginine apex.Sarah B. NyenhuisNakul KarandikarVolker KiesslingAlex J. B. KreutzbergerAnusa ThapaBinyong LiangLukas K. TammDavid S. CafisoNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-13 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Sarah B. Nyenhuis Nakul Karandikar Volker Kiessling Alex J. B. Kreutzberger Anusa Thapa Binyong Liang Lukas K. Tamm David S. Cafiso Conserved arginine residues in synaptotagmin 1 regulate fusion pore expansion through membrane contact
description	Synaptotagmin 1 (Syt1) is the calcium sensor for fast synchronous neurotransmitter release but the mechanism by which it functions is still under debate. Here, the authors combine EPR measurements and functional studies and observe that different faces of the Syt1 C2B domain play different roles in regulating neurotransmitter release and they show that the expansion of the fusion pore is mediated by membrane contact of the C2B arginine apex.
format	article
author	Sarah B. Nyenhuis Nakul Karandikar Volker Kiessling Alex J. B. Kreutzberger Anusa Thapa Binyong Liang Lukas K. Tamm David S. Cafiso
author_facet	Sarah B. Nyenhuis Nakul Karandikar Volker Kiessling Alex J. B. Kreutzberger Anusa Thapa Binyong Liang Lukas K. Tamm David S. Cafiso
author_sort	Sarah B. Nyenhuis
title	Conserved arginine residues in synaptotagmin 1 regulate fusion pore expansion through membrane contact
title_short	Conserved arginine residues in synaptotagmin 1 regulate fusion pore expansion through membrane contact
title_full	Conserved arginine residues in synaptotagmin 1 regulate fusion pore expansion through membrane contact
title_fullStr	Conserved arginine residues in synaptotagmin 1 regulate fusion pore expansion through membrane contact
title_full_unstemmed	Conserved arginine residues in synaptotagmin 1 regulate fusion pore expansion through membrane contact
title_sort	conserved arginine residues in synaptotagmin 1 regulate fusion pore expansion through membrane contact
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/81777fc5abd14f21a6ee0ae5308e9f0f
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Conserved arginine residues in synaptotagmin 1 regulate fusion pore expansion through membrane contact

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