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J. Biol. Chem., Vol. 280, Issue 3, 1962-1970, January 21, 2005

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Fyn Phosphorylates Human MAP-2c on Tyrosine 67^*

S. Pilar Zamora-Leon, Anne Bresnick, Jonathan M. Backer¶, and Bridget Shafit-Zagardo||

From the Departments of Pathology, Biochemistry, and ^¶Molecular Pharmacology, Albert Einstein College of Medicine, Bronx, New York 10461

The Src homology 3 (SH3) domain of Fyn binds to a conserved PXXP motif on microtubule-associated protein-2. Co-transfections into COS7 cells and in vitro kinase assays performed with Fyn and wild-type, or mutant MAP-2c, determined that Fyn phosphorylated MAP-2c on tyrosine 67. The phosphorylation generated a consensus sequence for the binding of the SH2 domain of Grb2 (pYSN). Pull-down assays with SH2-Grb2 from human fetal brain homogenates, and co-immunoprecipitation of Grb2 and MAP-2 confirmed the interaction in vivo, and demonstrated that MAP-2c is tyrosine-phosphorylated in human fetal brain. Filter overlay assays confirmed that the SH2 domain of Grb2 binds to human MAP-2c following incubation with active Fyn. Enzyme-linked immunosorbent assays confirmed the interaction between the SH2 domain of Grb2 and a tyrosine-phosphorylated MAP-2 peptide spanning the pY⁶⁷SN motif. Thus, MAP-2c can directly recruit multiple signaling proteins important for central nervous system development.

Received for publication, October 5, 2004 , and in revised form, November 4, 2004.

^* This work was supported by National Multiple Sclerosis Society Grant RG3020 (to B. S.-Z.) and National Institutes of Health Grants NS38102 (to B. S.-Z.) and GM55692 (to J. M. B.). The costs of publication of this article were defrayed in part by the payment of page charges. This 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 Pathology, Albert Einstein College of Medicine. Bronx, NY 10461. Tel.: 718-430-2189; Fax: 718-430-8541; E-mail: zagardo{at}aecom.yu.edu.

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