Title |
Synaptotagmin Interaction with the Syntaxin/SNAP-25 Dimer Is Mediated by an Evolutionarily Conserved Motif and Is Sensitive to Inositol Hexakisphosphate*
|
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Published in |
Journal of Biological Chemistry, January 2004
|
DOI | 10.1074/jbc.m310710200 |
Pubmed ID | |
Authors |
Colin Rickman, Deborah A. Archer, Frederic A. Meunier, Molly Craxton, Mitsunori Fukuda, Robert D. Burgoyne, Bazbek Davletov |
Abstract |
Synaptotagmins are membrane proteins that possess tandem C2 domains and play an important role in regulated membrane fusion in metazoan organisms. Here we show that both synaptotagmins I and II, the two major neuronal isoforms, can interact with the syntaxin/synaptosomal-associated protein of 25 kDa (SNAP-25) dimer, the immediate precursor of the soluble NSF attachment protein receptor (SNARE) fusion complex. A stretch of basic amino acids highly conserved throughout the animal kingdom is responsible for this calcium-independent interaction. Inositol hexakisphosphate modulates synaptotagmin coupling to the syntaxin/SNAP-25 dimer, which is mirrored by changes in chromaffin cell exocytosis. Our results shed new light on the functional importance of the conserved polybasic synaptotagmin motif, suggesting that synaptotagmin interacts with the t-SNARE dimer to up-regulate the probability of SNARE-mediated membrane fusion. |
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Geographical breakdown
Country | Count | As % |
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Japan | 1 | 1% |
United States | 1 | 1% |
Switzerland | 1 | 1% |
Unknown | 62 | 90% |
Demographic breakdown
Readers by professional status | Count | As % |
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Student > Ph. D. Student | 21 | 30% |
Researcher | 14 | 20% |
Professor > Associate Professor | 8 | 12% |
Student > Master | 6 | 9% |
Student > Bachelor | 5 | 7% |
Other | 8 | 12% |
Unknown | 7 | 10% |
Readers by discipline | Count | As % |
---|---|---|
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Biochemistry, Genetics and Molecular Biology | 11 | 16% |
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Neuroscience | 5 | 7% |
Chemistry | 3 | 4% |
Other | 4 | 6% |
Unknown | 8 | 12% |