作者: Jun Kitano , Yoshimitsu Yamazaki , Kouji Kimura , Tomoko Masukado , Yoshiaki Nakajima
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摘要: Tamalin is a scaffold protein that comprises multiple protein-interacting domains, including 95-kDa postsynaptic density (PSD-95)/discs-large/ZO-1 (PDZ) domain, leucine-zipper region, and carboxyl-terminal PDZ binding motif. forms complex with metabotropic glutamate receptors guanine nucleotide exchange factor cytohesins promotes intracellular trafficking cell surface expression of group 1 receptors. In the present study, using several different approaches we have shown tamalin interacts neuronal proteins through its distinct protein-binding domains. The domain binds to motifs SAP90/PSD-95-associated itself, whereas motif capable interacting S-SCAM. addition, PSD-95 Mint2/X11β/X11L by mechanisms from PDZ-mediated interaction. has ability assemble these proteinsin vivo; their was verified coimmunoprecipitation rat brain lysates. Interestingly, domains are evolutionarily conserved, mRNA developmentally up-regulated at postnatal period. results indicate exists as key element protein-trafficking proteins.