Sec1p directly stimulates SNARE-mediated membrane fusion in vitro.
Sec1p directly stimulates SNARE-mediated membrane fusion in vitro.
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DOI：
10.1083/jcb.200405018
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发表时间：
2004-10-11
期刊：
影响因子：
--
通讯作者：
McNew JA
中科院分区：
文献类型：
--
作者：
Scott BL;Van Komen JS;Irshad H;Liu S;Wilson KA;McNew JA
Sec1 proteins are critical players in membrane trafficking, yet their precise role remains unknown. We have examined the role of Sec1p in the regulation of post-Golgi secretion in Saccharomyces cerevisiae. Indirect immunofluorescence shows that endogenous Sec1p is found primarily at the bud neck in newly budded cells and in patches broadly distributed within the plasma membrane in unbudded cells. Recombinant Sec1p binds strongly to the t-SNARE complex (Sso1p/Sec9c) as well as to the fully assembled ternary SNARE complex (Sso1p/Sec9c;Snc2p), but also binds weakly to free Sso1p. We used recombinant Sec1p to test Sec1p function using a well-characterized SNARE-mediated membrane fusion assay. The addition of Sec1p to a traditional in vitro fusion assay moderately stimulates fusion; however, when Sec1p is allowed to bind to SNAREs before reconstitution, significantly more Sec1p binding is detected and fusion is stimulated in a concentration-dependent manner. These data strongly argue that Sec1p directly stimulates SNARE-mediated membrane fusion.
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