Distinct domains of complexin I differentially regulate neurotransmitter release
2007 | journal article; research paper. A publication with affiliation to the University of Göttingen.
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- Authors
- Xue, Mingshan; Reim, Kerstin; Chen, Xiaocheng; Chao, Hsiao-Tuan; Deng, Hui; Rizo, Josep; Brose, Nils ; Rosenmund, Christian
- Abstract
- Complexins constitute a family of four synaptic high-affinity SNARE complex-binding proteins. They positively regulate a late, post-priming step in Ca2+- triggered synchronous neurotransmitter release, but the underlying molecular mechanisms are unclear. We show here that SNARE complex binding of complexin I ( CplxI) via its central a-helix is necessary but, unexpectedly, not sufficient for its key function in promoting neurotransmitter release. An accessory alpha-helix on the N-terminal side of the SNARE complex-binding region has an inhibitory effect on fast synaptic exocytosis, whereas sequences N-terminally adjacent to this helix facilitate Ca2+- triggered release even in the absence of the Ca2+ sensor synaptotagmin-1. Our results indicate that distinct functional domains of CplxI differentially regulate synaptic exocytosis and that, through the interplay between these domains, CplxI carries out a crucial role in fine-tuning Ca2+- triggered fast neurotransmitter release.
- Issue Date
- 2007
- Publisher
- Nature Publishing Group
- Journal
- Nature Structural & Molecular Biology
- ISSN
- 1545-9985