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Distinct domains of complexin I differentially regulate neurotransmitter release
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Journal Article
Distinct domains of complexin I differentially regulate neurotransmitter release
2007
Overview
Complexins constitute a family of four synaptic high-affinity SNARE complex–binding proteins. They positively regulate a late, post-priming step in Ca
2+
-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 Ca
2+
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 Ca
2+
-triggered fast neurotransmitter release.
Publisher
Nature Publishing Group US,Nature Publishing Group
Subject
Adaptor Proteins, Vesicular Transport
/ Animals
/ Biomedical and Life Sciences
/ Mice
/ Nerve Tissue Proteins - chemistry
/ Nerve Tissue Proteins - genetics
/ Nerve Tissue Proteins - metabolism
/ Neurotransmitter Agents - metabolism
/ Presynaptic Terminals - metabolism
/ Protein Structure, Secondary
/ Proteins
/ Rats
/ Sucrose
/ Synaptic Transmission - physiology
