McMahon H T, Missler M, Li C, Südhof T C
Howard Hughes Medical Institute, University of Texas Southwestern Medical School, Dallas 75235, USA.
Cell. 1995 Oct 6;83(1):111-9. doi: 10.1016/0092-8674(95)90239-2.
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.
人们发现了一类名为突触结合蛋白的蛋白质家族，它们与α-SNAP竞争SNAP受体结合，但不与突触结合蛋白竞争。突触结合蛋白I和II是高度同源的亲水性蛋白质，保守性很强，小鼠、大鼠和人类的突触结合蛋白II之间有100%的同一性。它们在神经元中富集，与 syntaxin 和 SNAP-25 共定位；此外，突触结合蛋白II在低水平上普遍表达。突触结合蛋白单独与 syntaxin 结合较弱，与突触小泡蛋白和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竞争与核心复合物的结合，但不与包括突触结合蛋白I在内的其他相互作用分子竞争，这表明突触结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。
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