Synaptic scaffolding molecule interacts with axin |
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Authors: | Hirabayashi Susumu Nishimura Wataru Iida Junko Kansaku Ai Kishida Shosei Kikuchi Akira Tanaka Noriaki Hata Yutaka |
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Institution: | Department of Medical Biochemistry, Graduate School of Medicine, Tokyo Medical and Dental University, Tokyo, Japan. |
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Abstract: | 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 beta-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 GSK3beta-binding region of Axin. S-SCAM formed a complex with beta-catenin and Axin, but competed with GSK3beta for Axin-binding. Thereby, S-SCAM inhibited the Axin-mediated phosphorylation of beta-catenin by GSK3beta. |
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Keywords: | Axin β-catenin glycogen synthase kinase synaptic scaffolding molecule |
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