The scaffolding protein CASK mediates the interaction between rabphilin3a and β-neurexins

被引：36

作者：

Zhang, Y ^{[1
]}

Luan, ZD ^{[1
]}

Liu, AH ^{[1
]}

Hu, GX ^{[1
]}

机构：

[1] Chinese Acad Sci, Shanghai Inst Biol Sci, Max Planck Guest Lab, Inst Biochem & Cell Biol, Shanghai 200031, Peoples R China

来源：

FEBS LETTERS | 2001年 / 497卷 / 2-3期

关键词：

CASK; beta-neurexin; rabphilin3a; synaptic vesicle exocytosis; yeast two-hybrid system;

D O I：

10.1016/S0014-5793(01)02450-4

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

CASK, a member of the membrane-associated guanylate kinase (MAGUK) superfamily, binds to the carboxyl-terminus of beta -neurexins on the intracellular side of the presynaptic membrane. The guanylate kinase-like (GUK) domains of MAGUKs lack kinase activities, but might he important for mediating specific protein-protein interaction. By a yeast two-hybrid approach, we identified an interaction between the GUK domain of CASK and the C2B domain of rabphilin3a, a presynaptic protein involved in synaptic vesicle exocytosis. The interaction was confirmed by in vitro CST pull-down and co-immunoprecipitation assays. It,vas proposed that presynaptic vesicles might be guided to the vicinity of points of exocytosis defined by beta -neurexins via the interaction between rabphilin3a-CASK-beta -neurexins. (C) 2001 Federation of European Biochemical Societies. Published by Elsevier Science B,V. All rights reserved.

引用

页码：99 / 102

页数：4

共 28 条

[1] Better late than never: A role for rabs late in exocytosis [J].