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			PubMed Journals: Proc Natl Acad Sci U S A

  Source:		PMID: 8692915


    		Proc Natl Acad Sci U S A. 1996 Jul
     		9;93(14):6898-901.

			The stress response to ionizing radiation
			involoves c-Abl-dependent phosphorylation
			of SHPTP1.

			Kharbanda S(1), Bharti A, Pei D, Wang J,
			Pandey P, Ren R, Weichselbaum R, Walsh CT,
			Kufe D.

			Author Information
			(1) Division of Cancer Pharmacology,
			Dana-Farber Cancer Institute, Boston, MA
			02115, USA.

			c-Abl is a nonreceptor tyrosine kinase that
			is activated by certain DNA-damaging agents. The
			present studies demonstrate that nuclear
			c-Abl binds constitutively to the protein
			tyrosine phosphatase SHPTP1. Treatment with
			ionizing radiation is associated with
			c-Abl-dependent tyrosine phosphorylation
			of SHPTP1. The results demonstrate that
			the SH3 domain of c-Abl interacts with a
			WPDHGVPSEP motif (residues 417-426) in the
			catalytic domain of SHPTP1 and that c-Abl
			phosphorylates C terminal Y536 and Y564 sites.
			The functional significance of the c-Abl-SHPTP1
			interaction is supported by the demonstration
			that, like c-Abl, SHPTP1 regulates the induction
			of Jun kinase activity following DNA damage.
			These findings indicate that SHPTP1 is involved
			in the response to genotoxic stress through
			a c-Abl-dependent mechanism.

			PMCID: PMC38905 PMID: 8692915 [Indexed
			for MEDLINE]

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