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Synaptic scaffolding molecule interacts with Axin
Author(s) -
Hirabayashi Susumu,
Nishimura Wataru,
Iida Junko,
Kansaku Ai,
Kishida Shosei,
Kikuchi Akira,
Tanaka Noriaki,
Hata Yutaka
Publication year - 2004
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.2004.02497.x
Subject(s) - guanylate kinase , pdz domain , scaffold protein , immunoprecipitation , microbiology and biotechnology , phosphorylation , kinase , chemistry , biology , biochemistry , biophysics , signal transduction , membrane protein , gene , membrane
Synaptic scaffolding molecule (S‐SCAM) is a synaptic protein that consists of PDZ domains, a guanylate kinase domain, and WW domains. It interacts with N ‐methyl‐ d ‐aspartate receptor subunits, neuroligin, and β‐catenin. Here, we identified Axin as a novel binding partner of S‐SCAM. Axin was co‐immunoprecipitated with S‐SCAM from rat brain, detected in the post‐synaptic density fraction in rat brain subcellular fractionation, and partially co‐localized with S‐SCAM in neurons. The guanylate kinase domain of S‐SCAM directly bound to the GSK3β‐binding region of Axin. S‐SCAM formed a complex with β‐catenin and Axin, but competed with GSK3β for Axin‐binding. Thereby, S‐SCAM inhibited the Axin‐mediated phosphorylation of β‐catenin by GSK3β.