Nucleic Acids Research Advance Access originally published online on July 11, 2007
Nucleic Acids Research 2007 35(15):4941-4951; doi:10.1093/nar/gkm386
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Nucleic Acids Research, 2007, Vol. 35, No. 15 4941-4951
© 2007 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
Nucleic Acid Enzymes |
Cockayne syndrome protein B interacts with and is phosphorylated by c-Abl tyrosine kinase
1Laboratory of Molecular Gerontology, National Institutes on Aging, National Institutes of Health, Baltimore, MD 21224, USA, 2Research Resource Branch, National Institutes on Aging, National Institutes of Health, Baltimore, MD 21224, USA, 3Danish Center for Molecular Gerontology, MBI, University of Aarhus, Denmark and 4Dana-Farber Cancer Institute, Harvard Medical School, Boston, MA 02115, USA
*To whom correspondence should be addressed. Tel: +1-410-558-8162; Fax: +1-410-558-8157; Email: vbohr{at}nih.gov
Received February 19, 2007. Revised April 27, 2007. Accepted April 29, 2007.
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.
Present address: Syed Z. Imam, South Texas Veterans Health Care System and Departments of Medicine & Pharmacology, University of Texas, Health Science Center, San Antonio, TX, 78229,USA
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