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Synaptotagmin 1 clamps synaptic vesicle fusion in mammalian neurons independent of complexin

Author

Listed:
  • Nicholas A. Courtney

    (University of Wisconsin-Madison)

  • Huan Bao

    (University of Wisconsin-Madison)

  • Joseph S. Briguglio

    (University of Wisconsin-Madison)

  • Edwin R. Chapman

    (University of Wisconsin-Madison)

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.

Suggested Citation

  • Nicholas A. Courtney & Huan Bao & Joseph S. Briguglio & Edwin R. Chapman, 2019. "Synaptotagmin 1 clamps synaptic vesicle fusion in mammalian neurons independent of complexin," Nature Communications, Nature, vol. 10(1), pages 1-14, December.
    • Handle: RePEc:nat:natcom:v:10:y:2019:i:1:d:10.1038_s41467-019-12015-w
    DOI: 10.1038/s41467-019-12015-w
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