Journal
TRENDS IN BIOCHEMICAL SCIENCES
Volume 29, Issue 3, Pages 143-151Publisher
ELSEVIER SCIENCE LONDON
DOI: 10.1016/j.tibs.2004.01.008
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Funding
- NIGMS NIH HHS [GM56827] Funding Source: Medline
- NIMH NIH HHS [MH61876] Funding Source: Medline
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Rapid signaling between neurons relies on the Ca2+-triggered exocytosis of neurotransmitters. Release is mediated by 'kiss-and-run' or complete fusion of secretory organelles with the plasma membrane. Current models indicate that exocytosis is regulated by synaptotagmin I (syt) and mediated by SNARE (soluble NSF-attachment protein receptor) proteins. Syt senses Ca2+ via two conserved motifs, C2A and C2B. C2B engages a wider array of effector molecules than C2A and appears to play a more crucial role in synaptic transmission. However, it has recently become clear that the tandem C2 domains of syt influence each another in unexpected ways. Here, we focus on recent structure-function studies that are beginning to provide insights into the mechanism through which the C2 domains of syt trigger exocytosis.
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