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			PubMed Journals: J Biol Chem

  Source:		PMID: 10574931


    		J Biol Chem. 1999 Dec 3;274(49):34663-8.
     
			Functional interaction between SHPTP1 and
			the Lyn tyrosine kinase in the apoptotic
			response to DNA damage.

			Yoshida K(1), Kharbanda S, Kufe D.

			Author Information
			(1) Dana-Farber Cancer Institute,
			Harvard Medical School, Boston, Massachusetts
			02115, USA.

			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.

			PMID: 10574931 [Indexed for MEDLINE]

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