Cockayne Syndrome Protein B Interacts with and Is Phosphorylated by c-Abl Tyrosine Kinase

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Cockayne Syndrome Protein B Interacts with and Is Phosphorylated by c-Abl Tyrosine Kinase

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Title: Cockayne Syndrome Protein B Interacts with and Is Phosphorylated by c-Abl Tyrosine Kinase
Author: Inman, Syed Z.; Indig, Fred E.; Cheng, Wen-Hsing; Saxena, Satya P.; Stevnsner, Tinna; Kufe, Donald William; Bohr, Vilhelm A.

Note: Order does not necessarily reflect citation order of authors.

Citation: Imam, 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.
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Abstract: The 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.
Published Version: doi://10.1093/nar/gkm386
Other Sources: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1976445/pdf/
Terms of Use: This article is made available under the terms and conditions applicable to Other Posted Material, as set forth at http://nrs.harvard.edu/urn-3:HUL.InstRepos:dash.current.terms-of-use#LAA
Citable link to this page: http://nrs.harvard.edu/urn-3:HUL.InstRepos:4741826

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