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| Research article summary (published 23 May 2001): |
The scaffolding protein CASK mediates the interaction between rabphilin3a and beta-neurexins.
Full 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.
Author information
Author/s: Zhang, Y (Y); Luan, Z (Z); Liu, A (A); Hu, G (G);
Affiliation: 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.
Journal and publication information
Publication Type: Journal Article; Research Support, Non-U.S. Gov't
Journal: FEBS letters (FEBS Lett), published in Netherlands. (Language: eng)
Reference: 2001-May; vol 497 (issue 2-3) : pp 99-102
Dates: Created 2001/05/29; Completed 2001/07/05; Revised 2007/11/15;
PMID: 11377421, status: MEDLINE (last retrieval date: 2/18/2009, IMS Date: )
Sourced from the National Library of Medicine. Abstract text and other information may be subject to copyright.
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