Abstract：
:Synaptic vesicle (SV) exocytosis is mediated by SNARE proteins. Reconstituted SNAREs are constitutively active, so a major focus has been to identify fusion clamps that regulate their activity in synapses: the primary candidates are synaptotagmin (syt) 1 and complexin I/II. Syt1 is a Ca2+ sensor for SV release that binds Ca2+ via tandem C2-domains, C2A and C2B. Here, we first determined whether these C2-domains execute distinct functions. Remarkably, the C2B domain profoundly clamped all forms of SV fusion, despite synchronizing residual evoked release and rescuing the readily-releasable pool. Release was strongly enhanced by an adjacent C2A domain, and by the concurrent binding of complexin to trans-SNARE complexes. Knockdown of complexin had no impact on C2B-mediated clamping of fusion. We postulate that the C2B domain of syt1, independent of complexin, is the molecular clamp that arrests SVs prior to Ca2+-triggered fusion.
journal_name
Nat Communjournal_title
Nature communicationsauthors
Courtney NA,Bao H,Briguglio JS,Chapman ERdoi
10.1038/s41467-019-12015-wsubject
Has Abstractpub_date
2019-09-09 00:00:00pages
4076issue
1issn
2041-1723pii
10.1038/s41467-019-12015-wjournal_volume
10pub_type
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