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

FEBS Letters

Luan, Zhidong¹  Liu, Aihua¹  Zhang, Yan¹  Hu, Gengxi¹ 

[1] Max-Planck Guest Laboratory, Institute of Biochemistry and Cell Biology, Shanghai Institute for Biological Sciences, Chinese Academy of Sciences, 320, Yue-Yang Road, Shanghai 200031, PR China

关键词: CASK;    β-Neurexin;    Rabphilin3a;    Synaptic vesicle exocytosis;    Yeast two-hybrid system;    MAGUK;    membrane-associated guanylate kinase;    GUK;    guanylate kinase-like;    PSD;    postsynaptic density;    PDZ;    PSD-95/SAP90 discs large ZO-1 homologous;    SH3;    Src homology 3;    GKAP;    guanylate kinase domain-associated protein;    NMDAR;    N-methyl-D-aspartate receptor;   

DOI  :  10.1016/S0014-5793(01)02450-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

CASK, a member of the membrane-associated guanylate kinase (MAGUK) superfamily, binds to the carboxyl-terminus of β-neurexins on the intracellular side of the presynaptic membrane. The guanylate kinase-like (GUK) domains of MAGUKs lack kinase activities, but might be 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 GST pull-down and co-immunoprecipitation assays. It was proposed that presynaptic vesicles might be guided to the vicinity of points of exocytosis defined by β-neurexins via the interaction between rabphilin3a–CASK–β-neurexins.

【 授权许可】

Unknown