期刊
NATURE STRUCTURAL & MOLECULAR BIOLOGY
卷 17, 期 5, 页码 568-U65出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb.1791
关键词
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资金
- US National Institutes of Health [F31MH078678, NS037200, NS050655]
- Welch Foundation [I-1304]
- Baylor Research Advocates for Student Scientists and a McNair Fellowship
- Baylor College of Medicine Mental Retardation and Developmental Disabilities Research Center
Complexins facilitate and inhibit neurotransmitter release through distinct domains, and their function was proposed to be coupled to the Ca(2+) sensor synaptotagmin-1 (Syt1). However, the mechanisms underlying complexin function remain unclear. We now uncover an interaction between the complexin N terminus and the SNARE complex C terminus, and we show that disrupting this interaction abolishes the facilitatory function of complexins in mouse neurons. Analyses of hypertonically induced exocytosis show that complexins enhance synaptic-vesicle fusogenicity. Genetic experiments crossing complexin-and Syt1-null mice indicate a functional interaction between these proteins but also show that complexins can promote Ca(2+)-triggered release in the absence of Syt1. We propose that the complexin N terminus stabilizes the SNARE complex C terminus and/or helps release the inhibitory function of complexins, thereby activating the fusion machinery in a manner that may cooperate with Syt1 but does not require Syt1.
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