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J. Biol. Chem., Vol. 278, Issue 17, 14762-14768, April 25, 2003
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From the Department of Biological Sciences, Faculty of Medicine,
and the Department of Molecular and System Biology, Graduate School of
Biostudies, Kyoto University, Kyoto, 606-8501, Japan
Tamalin is a scaffold protein that comprises
multiple protein-interacting domains, including a 95-kDa
postsynaptic density protein (PSD-95)/discs-large/ZO-1 (PDZ)
domain, a leucine-zipper region, and a carboxyl-terminal PDZ
binding motif. Tamalin forms a complex with metabotropic glutamate
receptors and guanine nucleotide exchange factor cytohesins and
promotes intracellular trafficking and cell surface expression of group
1 metabotropic glutamate receptors. In the present study, using
several different approaches we have shown that tamalin interacts with
multiple neuronal proteins through its distinct protein-binding
domains. The PDZ domain of tamalin binds to the PDZ binding motifs of
SAP90/PSD-95-associated protein and tamalin itself, whereas the PDZ
binding motif of tamalin is capable of interacting with the PDZ domain
of S-SCAM. In addition, tamalin forms a complex with PSD-95 and
Mint2/X11
Tamalin Is a Scaffold Protein That Interacts with Multiple
Neuronal Proteins in Distinct Modes of Protein-Protein Association*
/X11L by mechanisms different from the PDZ-mediated
interaction. Tamalin has the ability to assemble with these proteins
in vivo; their protein complex with tamalin was verified by
coimmunoprecipitation of rat brain lysates. Interestingly, the distinct
protein-interacting domains of tamalin are evolutionarily conserved,
and mRNA expression is developmentally up-regulated at the
postnatal period. The results indicate that tamalin exists as a
key element that forms a protein complex with multiple postsynaptic and
protein-trafficking scaffold proteins.
*
This work was supported in part by research grants from the
Ministry of Education, Science, and Culture of Japan.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed. Tel.: 81-75-753-4437;
Fax: 81-75-753-4404; E-mail: snakanis@phy.med.kyoto-u.ac.jp.
Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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