Synaptotagmin-1 may be a distance regulator acting upstream of SNARE nucleation

被引：0

作者：

Geert van den Bogaart

Shashi Thutupalli

Jelger H Risselada

Karsten Meyenberg

Matthew Holt

Dietmar Riedel

Ulf Diederichsen

Stephan Herminghaus

Helmut Grubmüller

Reinhard Jahn

机构：

[1] Max Planck Institute for Biophysical Chemistry,Department of Neurobiology

[2] Max Planck Institute for Dynamics and Self-Organization,Department of Dynamics of Complex Fluids

[3] Max Planck Institute for Biophysical Chemistry,Department of Theoretical and Computational Biophysics

[4] Institute for Organic and Biomolecular Chemistry,undefined

[5] Georg-August University,undefined

[6] Facility for Electron Microscopy,undefined

[7] Max Planck Institute for Biophysical Chemistry,undefined

来源：

Nature Structural & Molecular Biology | 2011年 / 18卷

关键词：

D O I：

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学科分类号：

摘要：

Synaptotagmin-1 is known to accelerate membrane fusion during neuronal exocytosis in response to Ca2+, but how it does this is unclear. By probing the activity of synaptotagmin-1 under conditions of low ionic strength, it is now shown that SNARE-mediated fusion is dependent on synaptotagmin-1, which tethers liposomes together but at distances too far for fusion. Ca2+ then induces synaptotagmin-1 to bring the liposomes closer together, allowing fusion to proceed.

引用

页码：805 / 812

页数：7

共 22 条

[1] Synaptotagmin-1 may be a distance regulator acting upstream of SNARE nucleation
van den Bogaart, Geert
Thutupalli, Shashi
Risselada, Jelger H.
Meyenberg, Karsten
Holt, Matthew
Riedel, Dietmar
Diederichsen, Ulf
Herminghaus, Stephan
Grubmueller, Helmut
Jahn, Reinhard
NATURE STRUCTURAL & MOLECULAR BIOLOGY, 2011, 18 (07) : 805 - U82
[2] Dynamic binding mode of a Synaptotagmin-1–SNARE complex in solution
Kyle D Brewer
Taulant Bacaj
Andrea Cavalli
Carlo Camilloni
James D Swarbrick
Jin Liu
Amy Zhou
Peng Zhou
Nicholas Barlow
Junjie Xu
Alpay B Seven
Eric A Prinslow
Rashmi Voleti
Daniel Häussinger
Alexandre M J J Bonvin
Diana R Tomchick
Michele Vendruscolo
Bim Graham
Thomas C Südhof
Josep Rizo
Nature Structural & Molecular Biology, 2015, 22 : 555 - 564
[3] Synaptotagmin-1 Is an Antagonist for Munc18-1 in SNARE Zippering
Lou, Xiaochu
Shin, Jaeil
Yang, Yoosoo
Kim, Jaewook
Shin, Yeon-Kyun
JOURNAL OF BIOLOGICAL CHEMISTRY, 2015, 290 (16) : 10535 - 10543
[4] Synergistic regulation of fusion pore opening and dilation by SNARE and synaptotagmin-1
Li, Kaiju
Li, Kaiyu
Fan, Jiaqi
Zhang, Xing
Tao, Chengyan
Xiang, Yijuan
Cui, Lele
Li, Hao
Li, Minghan
Zhang, Yanjing
Geng, Jia
Lai, Ying
JOURNAL OF MOLECULAR CELL BIOLOGY, 2024, 16 (04)
[5] Analysis of SNARE Complex/Synaptotagmin-1 Interactions by One-Dimensional NMR Spectroscopy
Zhou, Amy
Brewer, Kyle D.
Rizo, Josep
BIOCHEMISTRY, 2013, 52 (20) : 3446 - 3456
[6] The neuronal calcium sensor Synaptotagmin-1 and SNARE proteins cooperate to dilate fusion pores
Wu, Zhenyong
Dharan, Nadiv
McDargh, Zachary A.
Thiyagarajan, Sathish
O'Shaughnessy, Ben
Karatekin, Erdem
ELIFE, 2021, 10
[7] Synaptotagmin-1 Utilizes Membrane Bending and SNARE Binding to Drive Fusion Pore Expansion
Lynch, Kara L.
Gerona, Roy R. L.
Kielar, Dana M.
Martens, Sascha
McMahon, Harvey T.
Martin, Thomas F. J.
MOLECULAR BIOLOGY OF THE CELL, 2008, 19 (12) : 5093 - 5103
[8] Synaptotagmin-1/Ca2+ Overcomes Inefficiency of SNARE Complex in Dilating the Fusion Pore
Khounlo, Ryan
BIOPHYSICAL JOURNAL, 2020, 118 (03) : 554A - 554A
[9] Structural Insight into the Interaction of Synaptotagmin-1 and Snare Complex on Lipid Bilayer by Cryo-Electron Microscopy
Grushin, Kirill
Wang, Jing
Coleman, Jeff
Rothman, James E.
Sindelar, Charles V.
Krishnakumar, Shyam S.
BIOPHYSICAL JOURNAL, 2018, 114 (03) : 282A - 282A
[10] Neurotransmitter release is triggered by a calcium- induced rearrangement in the Synaptotagmin-1/SNARE complex primary interface
Toulme, Estelle
Lazaro, Andrea Salazar
Trimbuch, Thorsten
Rizo, Josep
Rosenmund, Christian
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2024, 121 (42)

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