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J Biol Chem, Vol. 275, Issue 4, 2721-2726, January 28, 2000

Reciprocal Regulation of Hck Activity by Phosphorylation of Tyr527 and Tyr416
EFFECT OF INTRODUCING A HIGH AFFINITY INTRAMOLECULAR SH2 LIGAND*

Margaret PorterDagger , Thomas Schindler§, John Kuriyan§, and W. Todd MillerDagger par

From the Dagger  Department of Physiology and Biophysics, School of Medicine, State University of New York, Stony Brook, New York 11794-8661 and the § Laboratories of Molecular Biophysics,  Howard Hughes Medical Institute, Rockefeller University, New York, New York 10021

The Src family tyrosine kinase Hck possesses two phosphorylation sites, Tyr527 and Tyr416, that affect the catalytic activity in opposite ways. When phosphorylated, Tyr527 and residues C-terminal to it are involved in an inhibitory intramolecular interaction with the SH2 domain. However, this sequence does not conform to the sequence of the high affinity SH2 ligand, pYEEI. We mutated this sequence to YEEI and show that this mutant form of Hck cannot be activated by exogenous SH2 ligands. The SH3 domain of Hck is also involved in an inhibitory interaction with the catalytic domain. The SH3 ligand Nef binds to and activates YEEI-Hck mutant in a similar manner to wild-type Hck, indicating that disrupting the SH3 interaction overrides the strengthened SH2 interaction. The other phosphorylation site, Tyr416, is the autophosphorylation site in the activation loop. Phosphorylation of Tyr416 is required for Hck activation. We mutated this residue to alanine and characterized its catalytic activity. The Y416A mutant shows a higher Km value for peptide and a lower Vmax than autophosphorylated wild-type Hck. We also present evidence for cross-talk between the activation loop and the intramolecular binding of the SH2 and SH3 domains.

* This work was supported by National Institutes of Health Grant CA58530.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.

par To whom correspondence should be addressed: Dept. of Physiology and Biophysics, Basic Science Tower, T-6, School of Medicine, SUNY at Stony Brook, Stony Brook, NY 11794-8661. Tel.: 516-444-3533; Fax: 516-3444-3432; E-mail: miller@physiology.pnb.sunysb.edu.

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