Detection of c-Abl kinase-promoted phosphorylation of Rad51 by specific antibodies reveals that Y54 phosphorylation is dependent on that of Y315

Milena Popova, Hiroko Shimizu, Ken-ichi Yamamoto, Mickael Lebechec, Masayuki Takahashi, Fabrice Fleury

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13 Citations (Scopus)


Rad51 plays a crucial role in homologous recombination and recombinational DNA repair. Its activity is regulated by phosphorylation by the c-Abl kinase. Either Tyr54 or Tyr315 have been reported as the target of phosphorylation but the interconnection between their phosphorylation is not known. We prepared two specific antibodies that selectively detected the Tyr54 or Tyr315 phosphorylation site of Rad51. By co-transfection of HeLa cells with c-Abl and Rad51, we clearly showed that both Tyr54 and Tyr315 of Rad51 are phosphorylated by c-Abl. Furthermore, we showed that the phosphorylation of Tyr315 stimulates that of Tyr54, which indicates that the phosphorylation of Rad51 by the c-Abl kinase is a sequential process. Structured summary: MINT-7034009: cABL (uniprotkb:P00519) physically interacts (MI:0218) with RAD51 (uniprotkb:Q06609) by pull down (MI:0096).

Original languageEnglish
Pages (from-to)1867-1872
Number of pages6
JournalFEBS Letters
Issue number12
Publication statusPublished - Jun 18 2009
Externally publishedYes



  • Antibody purification
  • c-Abl tyrosine kinase
  • Homologous recombination
  • Phosphorylation
  • Rad51 protein

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Cell Biology
  • Genetics
  • Molecular Biology
  • Structural Biology

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