Cockayne Syndrome Protein B Interacts with and Is Phosphorylated by c-Abl Tyrosine Kinase
Inman, Syed Z.
Indig, Fred E.
Saxena, Satya P.
Bohr, Vilhelm A.Note: Order does not necessarily reflect citation order of authors.
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CitationImam, Syed Z., Fred E. Indig, Wen-Hsing Cheng, Satya P. Saxena, Tinna Stevnsner, Donald Kufe, and Vilhelm A. Bohr. 2007. Cockayne syndrome protein B interacts with and is phosphorylated by c-Abl tyrosine kinase. Nucleic Acids Research 35(15): 4941-4951.
AbstractThe Cockayne Syndrome group B (CSB) protein plays important roles in transcription, transcription-coupled nucleotide excision repair and base excision DNA repair. c-Abl kinase also plays a role in DNA repair as a regulator/coordinator of the DNA damage response. This study presents evidence that the N-terminal region of CSB interacts with the SH3 domain of c-Abl in vitro and in vivo. In addition, c-Abl kinase phosphorylates CSB at Tyr932. The subcellular localization of CSB to the nucleus and nucleolus is altered after phosphorylation by c-Abl. c-Abl-dependent phosphorylation of CSB increased in cells treated with hydrogen peroxide and decreased in cells pre-treated with STI-571, a c-Abl-specific protein kinase inhibitor. Activation of the c-Abl kinase in response to oxidative damage is not observed in CSB null cells. These results suggest that c-Abl and CSB may regulate each other in a reciprocal manner in response to oxidative stress.
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