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Vesicles returning from the Golgi to the ER need a GTPase called Arf1, and a coat called coatomer. But most of all they need vesicle SNAREs (v-SNAREs), which pair up with target SNAREs (t-SNAREs) to mediate fusion once the vesicles reach their destination. Now, Rein et al. report that a surprising conformational change lies behind the incorporation of v-SNAREs into the forming vesicles (page 395). K# Y! s6 f9 i5 S% [
0 `+ \6 d) \) t. S/ }) S. y4 ?) x X" LRein et al. begin with the observation that Arf1p's GTPase-activating protein, ARF-GAP, recruits Arf1p to membranes. ARF-GAP must be added first to get subsequent binding of Arf1p and coatomer, but ARF-GAP does not have to be present during the binding of Arf1p. Rather, it seems that ARF-GAP induces a conformational change in the v-SNARE proteins (converting them to a protease-resistant form), thus allowing Arf1p and coatomer to bind.
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This conformation-altering function is separable from the later GAP function of ARF-GAP, and it distinguishes the Golgi-to-ER system from the ER-to-Golgi system. In the latter case, v-SNAREs are taken up into vesicles via direct interactions with coat proteins, but there is no evidence for a conformational change.(ARF-GAP primes SNAREs to receive Arf1p.) |
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发表于 2009-3-6 00:09
发表于 2024-5-8 21:14
