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			PubMed Journals: J Biol Chem

  Source:		PMID: 10212258


    		J Biol Chem. 1999 Apr 30;274(18):12748-52.
     
			Radiation-induced assembly of Rad51 and
			Rad52 recombination complex requires ATM
			and c-Abl.

			Chen G(1), Yuan SS, Liu W, Xu Y, Trujillo
			K, Song B, Cong F, Goff SP, Wu Y, Arlinghaus
			R, Baltimore D, Gasser PJ, Park MS, Sung
			P, Lee EY.

			Author Information
			(1) Department of Molecular Medicine/Institute
			of Biotechnology,
			The University of Texas Health Science Center at San Antonio,
			San Antonio, Texas 78245, USA.

			Cells from individuals with the recessive
			cancer-prone disorder ataxia telangiectasia
			(A-T) are hypersensitive to ionizing radiation
			(I-R). ATM (mutated in A-T) is a protein
			kinase whose activity is stimulated by I-R.
			c-Abl, a nonreceptor tyrosine kinase, interacts
			with ATM and is activated by ATM following
			I-R. Rad51 is a homologue of bacterial RecA
			protein required for DNA recombination and
			repair. Here we demonstrate that there is
			an I-R-induced Rad51 tyrosine phosphorylation,
			and this induction is dependent on both
			ATM and c-Abl. ATM, c-Abl, and Rad51 can
			be co-immunoprecipitated from cell extracts.
			Consistent with the physical interaction,
			c-Abl phosphorylates Rad51 in vitro and
			in vivo. In assays using purified components,
			phosphorylation of Rad51 by c-Abl enhances
			complex formation between Rad51 and Rad52,
			which cooperates with Rad51 in recombination
			and repair. After I-R, an increase in association
			between Rad51 and Rad52 occurs in wild-type
			cells but not in cells with mutations that
			compromise ATM or c-Abl. Our data suggest
			signaling mediated through ATM, and c-Abl
			is required for the correct post-translational
			modification of Rad51, which is critical
			for the assembly of Rad51 repair protein
			complex following I-R.

			PMID: 10212258 [Indexed for MEDLINE]

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