Pfeffer S R
Department of Biochemistry, Stanford University School of Medicine, CA 94305-5307.
Curr Opin Cell Biol. 1994 Aug;6(4):522-6. doi: 10.1016/0955-0674(94)90071-x.
Rab GTPases are thought to be likely to catalyze the accurate association of pairs of targeting molecules located on the surfaces of transport vesicles with their corresponding membrane acceptors. Advances during the past year have solidified our understanding of the mechanisms by which Rab proteins are recruited onto nascent transport vesicles and retrieved from their fusion targets. Functional analyses of Rab proteins in living cells have led to the surprising observation that vesicles do not seem to form if the appropriate Rab protein, in its GTP-bound conformation, is not present.
Rab GTP酶被认为可能催化位于运输囊泡表面的成对靶向分子与其相应膜受体的精确结合。过去一年的进展巩固了我们对Rab蛋白被招募到新生运输囊泡上并从其融合靶点回收的机制的理解。对活细胞中Rab蛋白的功能分析得出了一个惊人的观察结果：如果不存在处于GTP结合构象的合适Rab蛋白，囊泡似乎就不会形成。
