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The scaffolding protein CASK mediates the interaction between rabphilin3a and β‐neurexins
Author(s) -
Zhang Yan,
Luan Zhidong,
Liu Aihua,
Hu Gengxi
Publication year - 2001
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(01)02450-4
Subject(s) - cask , guanylate kinase , microbiology and biotechnology , scaffold protein , exocytosis , neurexin , biology , synaptic vesicle , immunoprecipitation , vesicle , membrane protein , biochemistry , signal transduction , membrane , genetics , receptor , postsynaptic potential , gene
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.