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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Adaptor Proteins, Signal Transducing
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Animals
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Blotting, Western
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COS Cells
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Calcium-Calmodulin-Dependent Protein Kinases*
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Exocytosis
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Glutathione Transferase / genetics
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Glutathione Transferase / metabolism
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Guanylate Kinases
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Nerve Tissue Proteins / metabolism*
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Nucleoside-Phosphate Kinase / metabolism*
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Nucleoside-Phosphate Kinase / pharmacology
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Precipitin Tests
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Protein Binding / drug effects
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Protein Binding / physiology
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Protein Isoforms / metabolism
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Protein Structure, Tertiary / physiology
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Rabphilin-3A
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Recombinant Fusion Proteins / genetics
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Recombinant Fusion Proteins / metabolism
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Synaptic Vesicles / metabolism
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Two-Hybrid System Techniques
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Vesicular Transport Proteins
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rab GTP-Binding Proteins / metabolism*
Substances
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Adaptor Proteins, Signal Transducing
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Nerve Tissue Proteins
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Protein Isoforms
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Recombinant Fusion Proteins
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Vesicular Transport Proteins
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neurexin II
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neurexin IIIbeta
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neurexin Ibeta
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Glutathione Transferase
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CASK kinases
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Calcium-Calmodulin-Dependent Protein Kinases
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Nucleoside-Phosphate Kinase
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Guanylate Kinases
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rab GTP-Binding Proteins