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Ypt1p参与v-SNARE激活。

Ypt1p implicated in v-SNARE activation.

作者信息

Lian J P, Stone S, Jiang Y, Lyons P, Ferro-Novick S

机构信息

Department of Cell Biology, Yale University Medical School, New Haven, Connecticut 06510.

出版信息

Nature. 1994 Dec 15;372(6507):698-701. doi: 10.1038/372698a0.

Abstract

Synaptobrevin-like membrane proteins that reside on transport vesicles, called the vesicle SNARE (v-SNARE), play a key role in ensuring that a vesicle targets and fuses with its correct acceptor compartment. Here we show that Bos1p, the v-SNARE of yeast endoplasmic reticulum-to-Golgi transport vesicles, pairs with another integral membrane protein of similar topology (Sec22p) on vesicles. This pairing, which appears to require functional Ypt1p (Rab in mammalian cells), may aid the activity of Bos1p on this compartment. These findings suggest that Rabs regulate the specificity of membrane fusion by selectively activating the v-SNARE on carrier vesicles. Because the v-SNARE resides on more than one membrane, such a regulated activation step may be necessary to prevent the premature fusion of donor and acceptor compartments.

摘要

位于运输小泡上的类似突触小泡蛋白的膜蛋白,即小泡SNARE(v-SNARE),在确保小泡靶向并与其正确的受体区室融合方面起着关键作用。我们在此表明,酵母内质网到高尔基体运输小泡的v-SNARE Bos1p,与小泡上另一种拓扑结构相似的整合膜蛋白(Sec22p)配对。这种配对似乎需要功能性的Ypt1p(哺乳动物细胞中的Rab),可能有助于Bos1p在该区室发挥作用。这些发现表明,Rabs通过选择性激活载体小泡上的v-SNARE来调节膜融合的特异性。由于v-SNARE存在于不止一种膜上,这样一个受调控的激活步骤对于防止供体和受体区室过早融合可能是必要的。

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