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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Auteurs principaux:	Sarah B. Nyenhuis, Nakul Karandikar, Volker Kiessling, Alex J. B. Kreutzberger, Anusa Thapa, Binyong Liang, Lukas K. Tamm, David S. Cafiso
Format:	article
Langue:	EN
Publié:	Nature Portfolio 2021
Sujets:	Science Q
Accès en ligne:	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
work_keys_str_mv	AT sarahbnyenhuis conservedarginineresiduesinsynaptotagmin1regulatefusionporeexpansionthroughmembranecontact AT nakulkarandikar conservedarginineresiduesinsynaptotagmin1regulatefusionporeexpansionthroughmembranecontact AT volkerkiessling conservedarginineresiduesinsynaptotagmin1regulatefusionporeexpansionthroughmembranecontact AT alexjbkreutzberger conservedarginineresiduesinsynaptotagmin1regulatefusionporeexpansionthroughmembranecontact AT anusathapa conservedarginineresiduesinsynaptotagmin1regulatefusionporeexpansionthroughmembranecontact AT binyongliang conservedarginineresiduesinsynaptotagmin1regulatefusionporeexpansionthroughmembranecontact AT lukasktamm conservedarginineresiduesinsynaptotagmin1regulatefusionporeexpansionthroughmembranecontact AT davidscafiso conservedarginineresiduesinsynaptotagmin1regulatefusionporeexpansionthroughmembranecontact
_version_	1718392031422709760

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

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