Synaptotagmin Interaction with the Syntaxin/SNAP-25 Dimer Is Mediated by an Evolutionarily Conserved Motif and Is Sensitive to Inositol Hexakisphosphate

Colin Rickman, Deborah A. Archer, Frederic A. Meunier, Molly Craxton, Mitsunori Fukuda, Robert D. Burgoyne, Bazbek Davletov

研究成果: ジャーナルへの寄稿学術論文査読

106 被引用数 (Scopus)

抄録

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.

本文言語英語
ページ(範囲)12574-12579
ページ数6
ジャーナルJournal of Biological Chemistry
279
13
DOI
出版ステータス出版済み - 2004 3月 26

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