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Synaptotagmin arrests the SNARE complex before triggering fast, efficient membrane fusion in response to Ca2+.

Abstract：

:Neuronal communication is mediated by Ca(2+)-triggered fusion of transmitter-filled synaptic vesicles with the presynaptic plasma membrane. Synaptotagmin I functions as a Ca(2+) sensor that regulates exocytosis, whereas soluble N-ethylmaleimide-sensitive factor attachment protein (SNAP) receptor (SNARE) proteins in the vesicle and target membrane assemble into complexes that directly catalyze bilayer fusion. Here we report that, before the Ca(2+) trigger, synaptotagmin interacts with SNARE proteins in the target membrane to halt SNARE complex assembly at a step after donor vesicles attach, or dock, to target membranes. This results in fusion complexes that, when subsequently triggered by Ca(2+), drive rapid, highly efficient lipid mixing. Ca(2+)-independent interactions with SNAREs also predispose synaptotagmin to selectively penetrate the target membrane in response to Ca(2+); we demonstrate that Ca(2+)-synaptotagmin must insert into the target membrane to accelerate SNARE-catalyzed fusion. These findings demonstrate that Ca(2+) converts synaptotagmin from a clamp to a trigger for exocytosis.

journal_name

Nat Struct Mol Biol

journal_title

Nature structural & molecular biology

authors

Chicka MC,Hui E,Liu H,Chapman ER

doi

10.1038/nsmb.1463

subject

Has Abstract

pub_date

2008-08-01 00:00:00

pages

827-35

issue

8

eissn

1545-9993

issn

1545-9985

pii

nsmb.1463

journal_volume

15

pub_type

杂志文章

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