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Cockayne syndrome protein B interacts with and is phosphorylated by c-Abl tyrosine kinase.


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.

SUBMITTER: Imam SZ 

PROVIDER: S-EPMC1976445 | biostudies-literature | 2007

REPOSITORIES: biostudies-literature

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Cockayne syndrome protein B interacts with and is phosphorylated by c-Abl tyrosine kinase.

Imam Syed Z SZ   Indig Fred E FE   Cheng Wen-Hsing WH   Saxena Satya P SP   Stevnsner Tinna T   Kufe Donald D   Bohr Vilhelm A VA  

Nucleic acids research 20070711 15


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 nu  ...[more]

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