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J Biol Chem, Vol. 274, Issue 49, 34663-34668, December 3, 1999

Functional Interaction between SHPTP1 and the Lyn Tyrosine Kinase in the Apoptotic Response to DNA Damage

Kiyotsugu Yoshida, Surender Kharbanda, and Donald Kufe

From the Dana-Farber Cancer Institute, Harvard Medical School, Boston, Massachusetts 02115

The Lyn protein-tyrosine kinase is activated in the cellular response to DNA-damaging agents. Here we demonstrate that Lyn associates constitutively with the SHPTP1 protein-tyrosine phosphatase. The SH3 domain of Lyn interacts directly with SHPTP1. The results show that Lyn phosphorylates SHPTP1 at the C-terminal Tyr-564 site. Lyn-mediated phosphorylation of SHPTP1 stimulates SHPTP1 tyrosine phosphatase activity. We also demonstrate that treatment of cells with 1-beta -D-arabinofuranosylcytosine and other genotoxic agents induces Lyn-dependent phosphorylation and activation of SHPTP1. The significance of the Lyn-SHPTP1 interaction is supported by the demonstration that activation of Lyn contributes in part to the apoptotic response to ara-C treatment and that SHPTP1 attenuates this response. These findings support a functional interaction between Lyn and SHPTP1 in the response to DNA damage.

Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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