The BioGRID | PUBLICATION VIEW

	FEBS Lett. May (2001); 497(2):99-102
The scaffolding protein CASK mediates the interaction between rabphilin3a and beta-neurexins.
Zhang Y, Luan Z, Liu A, Hu G
Max-Planck Guest Laboratory, Institute of Biochemistry and Cell Biology, Shanghai Institute for Biological Sciences, Chinese Academy of Sciences, 320, Yue-Yang Road, 200031, Shanghai, PR China.
Abstract: 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 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 beta-neurexins via the interaction between rabphilin3a-CASK-beta-neurexins.
[PUBMED: 11377421]