Models of synaptotagmin-1 to trigger Ca<sup>2+</sup>-dependent vesicle fusion

Review (2018)

Authors

Yongsoo Park Koç University
J.K. Ryu Kavli institute of nanoscience Delft, BN/Cees Dekker Lab - AS
Research Group
BN/Cees Dekker Lab (AS) (TU Delft)
Copyright: © 2018 Yongsoo Park, J.K. Ryu
DOI
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https://doi.org/10.1002/1873-3468.13193
Vesicle fusion Complexin Neurotransmitter Peptide hormone SNARE Synaptotagmin-1
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Published Date

2018

Language

English

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Faculty

Applied Sciences

Department

BN/Bionanoscience

Research Group

BN/Cees Dekker Lab

Abstract

Vesicles in neurons and neuroendocrine cells store neurotransmitters and peptide hormones, which are released by vesicle fusion in response to Ca2+-evoking stimuli. Synaptotagmin-1 (Syt1), a Ca2+ sensor, mediates ultrafast exocytosis in neurons and neuroendocrine cells. After vesicle docking, Syt1 has two main groups of binding partners: anionic phospholipids and the SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptors) complex. The molecular mechanisms by which Syt1 triggers vesicle fusion remain controversial. This Review introduces and summarizes six molecular models of Syt1: (a) Syt1 triggers SNARE unclamping by displacing complexin, (b) Syt1 clamps SNARE zippering, (c) Syt1 causes membrane curvature, (d) membrane bridging by Syt1, (e) Syt1 is a vesicle-plasma membrane distance regulator, and (f) Syt1 undergoes circular oligomerization. We discuss important conditions to test Syt1 activity in vitro and attempt to illustrate the possible roles of Syt1.