Regulation of Rad51 function by c-Abl in response to DNA damage

Zhi Min Yuan, Yinyin Huang, Takatoshi Ishiko, Shuji Nakada, Taiju Utsugisawa, Surender Kharbanda, Rong Wang, Patrick Sung, Akira Shinohara, Ralph Weichselbaum, Donald Kufe

Research output: Contribution to journalArticle

174 Scopus citations

Abstract

The Rad51 protein, a homolog of bacterial RecA, functions in DNA double- strand break repair and genetic recombination. Whereas Rad51 catalyzes ATP- dependent pairing and strand exchange between homologous DNA molecules, regulation of this function is unknown. The c-Abl tyrosine kinase is activated by ionizing radiation and certain other DNA-damaging agents. Here we demonstrate that c-Abl interacts constitutively with Rad51. We show that c-Abl phosphorylates Rad51 on Tyr-54 in vitro. The results also show that treatment of cells with ionizing radiation induces c-Abl-dependent phosphorylation of Rad51. Phosphorylation of Rad51 by c-Abl inhibits the binding of Rad51 to DNA and the function of Rad51 in ATP-dependent DNA strand exchange reactions. These findings represent the first demonstration that Rad51 is regulated by phosphorylation and support a functional role for c- Abl in regulating Rad51-dependent recombination in the response to DNA damage.

Original languageEnglish (US)
Pages (from-to)3799-3802
Number of pages4
JournalJournal of Biological Chemistry
Volume273
Issue number7
DOIs
StatePublished - Feb 13 1998

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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    Yuan, Z. M., Huang, Y., Ishiko, T., Nakada, S., Utsugisawa, T., Kharbanda, S., Wang, R., Sung, P., Shinohara, A., Weichselbaum, R., & Kufe, D. (1998). Regulation of Rad51 function by c-Abl in response to DNA damage. Journal of Biological Chemistry, 273(7), 3799-3802. https://doi.org/10.1074/jbc.273.7.3799