Cockayne syndrome protein B interacts with and is phosphorylated by c-Abl tyrosine kinase
| Autor: | Satya Saxena, Donald Kufe, Fred E. Indig, Tinna Stevnsner, Wen-Hsing Cheng, Syed Z. Imam, Vilhelm A. Bohr |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2007 |
| Předmět: |
musculoskeletal diseases
congenital hereditary and neonatal diseases and abnormalities medicine.drug_class DNA damage DNA repair Biology SH3 domain Cockayne syndrome Cell Line Mice hemic and lymphatic diseases Genetics medicine Animals Humans Phosphorylation Poly-ADP-Ribose Binding Proteins Proto-Oncogene Proteins c-abl neoplasms Cells Cultured Kinase Nucleic Acid Enzymes DNA Helicases nutritional and metabolic diseases Protein kinase inhibitor medicine.disease Cell biology Oxidative Stress Imatinib mesylate DNA Repair Enzymes Biochemistry Tyrosine Nucleotide excision repair |
| Zdroj: | Nucleic Acids Research |
| ISSN: | 1362-4962 0305-1048 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|