Article abstract
Nature Structural & Molecular Biology 14, 949 - 958 (2007)
Published online: 9 September 2007 | doi:10.1038/nsmb1292
Distinct domains of complexin I differentially regulate neurotransmitter release
Mingshan Xue1,4, Kerstin Reim2,4, Xiaocheng Chen3, Hsiao-Tuan Chao1, Hui Deng1, Josep Rizo3, Nils Brose2 & Christian Rosenmund1
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 
-helix is necessary but, unexpectedly, not sufficient for its key function in promoting neurotransmitter release. An accessory -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.
- Department of Neuroscience and Department of Molecular and Human Genetics, Baylor College of Medicine, Houston, Texas 77030, USA.
- Department of Molecular Neurobiology, Max Planck Institute of Experimental Medicine, D-37075 Göttingen, Germany.
- Department of Biochemistry and Department of Pharmacology, University of Texas Southwestern Medical Center, Dallas, Texas 75390, USA.
- These authors contributed equally to this work.
Correspondence to: Nils Brose2 e-mail: brose@em.mpg.de
Correspondence to: Christian Rosenmund1 e-mail: rosenmun@bcm.tmc.edu
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