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Originally published In Press as doi:10.1074/jbc.M909302199 on March 16, 2000

J. Biol. Chem., Vol. 275, Issue 21, 16167-16173, May 26, 2000
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The Protein-tyrosine Phosphatase PTPMEG Interacts with Glutamate Receptor delta 2 and epsilon  Subunits*

Katsunori HironakaDagger , Hisashi UmemoriDagger , Tohru TezukaDagger , Masayoshi Mishina§, and Tadashi YamamotoDagger

From the Dagger  Department of Oncology, Institute of Medical Science, University of Tokyo, Minato-ku, Tokyo 108-8639, the § Department of Molecular Neurobiology and Pharmacology, School of Medicine, University of Tokyo, Tokyo 113-8655, and CREST, Japan Science and Technology Corporation, Saitama 322-0012, Japan

Glutamate receptor (GluR) delta 2 is selectively expressed in cerebellar Purkinje cells and plays a crucial role in cerebellum-dependent motor learning. Although GluRdelta 2 belongs to an ionotropic GluR family, little is known about its pharmacological features and downstream signaling cascade. To study molecular mechanisms underlying GluRdelta 2-dependent motor learning, we employed yeast two-hybrid screening to isolate GluRdelta 2-interacting molecules and identified protein-tyrosine phosphatase PTPMEG. PTPMEG is a family member of band 4.1 domain-containing protein-tyrosine phosphatases and is expressed prominently in brain. Here, we showed by in situ hybridization analysis that the PTPMEG mRNA was enriched in mouse thalamus and Purkinje cells. We also showed that PTPMEG interacted with GluRdelta 2 as well as with N-methyl-D-aspartate receptor GluRepsilon 1 in cultured cells and in brain. PTPMEG bound to the putative C-terminal PDZ target sequence of GluRdelta 2 and GluRepsilon 1 via its PDZ domain. Examination of the effect of PTPMEG on tyrosine phosphorylation of GluRepsilon 1 unexpectedly revealed that PTPMEG enhanced Fyn-mediated tyrosine phosphorylation of GluRepsilon 1 in its PTPase activity-dependent manner. Thus, we conclude that PTPMEG associates directly with GluRdelta 2 and GluRepsilon 1. Moreover, our data suggest that PTPMEG plays a role in signaling downstream of the GluRs and/or in regulation of their activities through tyrosine dephosphorylation.

* This work was supported by grants from the Ministry of Education, Science, Sports, and Culture of Japan and from the Organization for Pharmaceutical Safety and Research 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: Dept. of Oncology, Inst. of Medical Science, University of Tokyo, Minato-ku, Tokyo 108-8639, Japan. Tel.: 81-3-5449-5301; Fax: 81-3-5449-5413; E-mail: tyamamot@ims.u-tokyo.ac.jp.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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