Distinct domains of complexin I differentially regulate neurotransmitter release

Mingshan Xue, Kerstin Reim, Xiaocheng Chen, Hsiao Tuan Chao, Hui Deng, Jose Rizo-Rey, Nils Brose, Christian Rosenmund

Research output: Contribution to journalArticlepeer-review

164 Scopus citations


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 α-helix is necessary but, unexpectedly, not sufficient for its key function in promoting neurotransmitter release. An accessory α-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 Ca 2+-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.

Original languageEnglish (US)
Pages (from-to)949-958
Number of pages10
JournalNature Structural and Molecular Biology
Issue number10
StatePublished - Oct 2007

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology


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