COMPLEXINS - CYTOSOLIC PROTEINS THAT REGULATE SNAP RECEPTOR FUNCTION
COMPLEXINS - CYTOSOLIC PROTEINS THAT REGULATE SNAP RECEPTOR FUNCTION
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DOI：
10.1016/0092-8674(95)90239-2
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发表时间：
1995-10-06
期刊：
影响因子：
64.5
通讯作者：
SUDHOF, TC
中科院分区：
文献类型：
--
作者：
MCMAHON, HT;MISSLER, M;SUDHOF, TC
发现了一个称为复合蛋白的蛋白质家族，它与α-SNAP竞争SNAP受体结合，但不与突触结合蛋白竞争。复合蛋白I和II是高度同源的亲水性蛋白质，它们是高度保守的，在小鼠、大鼠和人复合蛋白II之间具有100%的同一性。它们在神经元中富集，在那里它们与突触融合蛋白和SNAP-25共定位;此外，复合蛋白II以低水平普遍表达。复合蛋白仅与突触融合蛋白弱结合，而与小突触蛋白和SNAP-25完全不结合，但与由这三种分子组成的SNAP受体核心复合物强烈结合。它们与α-SNAP竞争结合核心复合物，但不与其他相互作用的分子，包括突触结合蛋白I，这表明复合蛋白在胞吐过程中调节α-SNAP和突触结合蛋白与SNAP受体的顺序相互作用。
A family of proteins called complexins was discovered that compete with alpha-SNAP, but not synaptotagmin, for SNAP receptor binding. Complexins I and II are highly homologous hydrophilic proteins that are tightly conserved, with 100% identity among mouse, rat, and human complexin II. They are enriched in neurons where they colocalize with syntaxin and SNAP-25; in addition, complexin II is expressed ubiquitously at low levels. Complexins bind weakly to syntaxin alone and not at all to synaptobrevin and SNAP-25, but strongly to the SNAP receptor-core complex composed of these three molecules. They compete with alpha-SNAP for binding to the core complex but not with other interacting molecules, including synaptotagmin I, suggesting that the complexins regulate the sequential interactions of alpha-SNAP and synaptotagmins with the SNAP receptor during exocytosis.