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M208151200v1
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Papers In Press, published online ahead of print October 11, 2002
J. Biol. Chem, 10.1074/jbc.M208151200
Submitted on August 9, 2002
Revised on October 7, 2002
Accepted on October 11, 2002

Regulation of ionizing radiation-induced Rad52 nuclear foci formation by c-Abl-mediated phosphorylation

Hiroyuki Kitao and Zhi-Min Yuan

Cancer Cell Biology, Harvard School of Public Health, Boston, MA 02115

Corresponding Author: zyuan{at}hsph.harvard.edu

The RAD52 epistasis group of proteins, including Rad51, Rad52 and Rad54, play an important role in the homologous recombination repair of double strand breaks (DSBs). A well-characterized feature associated with the ability of these proteins to repair DSBs is the inducible nuclear foci formation at the sites of damage. How the process is functionally regulated in response to DNA damage, however, remains elusive. We show here that the c-Abl tyrosine kinase associates with and phosphorylates Rad52 on tyrosine 104. Importantly, the very same site of Rad52 is phosphorylated upon exposure of cells to ionizing radiation (IR). Functional significance of c-Abl-dependent phosphorylation of Rad52 is underscored by our findings that cells expressing the phosphorylation-resistant Rad52 mutant, where the 104-tyrosine was replaced by phenylalanine, exhibit compromised nuclear foci formation in response to IR. Furthermore, IR-induced Rad52 nuclear foci formation is markedly suppressed by the expression of dominant negative c-Abl. Together, our data support a mode of post-translational regulation of Rad52 mediated by the c-Abl tyrosine kinase.


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