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- W1983702397 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." @default.
- W1983702397 created "2016-06-24" @default.
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- W1983702397 date "2001-05-22" @default.
- W1983702397 modified "2023-09-26" @default.
- W1983702397 title "The scaffolding protein CASK mediates the interaction between rabphilin3a and β-neurexins" @default.
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- W1983702397 doi "https://doi.org/10.1016/s0014-5793(01)02450-4" @default.
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