Determination of cell fate by c-Abl activation in the response to DNA damage

• Published in: Oncogene Vol. 17; no. 25; pp. 3309 - 3318
• Main Authors: Kharbanda, S, Yuan, Z M, Weichselbaum, R, Kufe, D
• Format: Journal Article
• Language: English
• Published: England Nature Publishing Group 24.12.1998
• Subjects: 1-Phosphatidylinositol 3-kinase; Abl protein; Animals; Apoptosis; Apoptosis - genetics; Ataxia telangiectasia; Ataxia telangiectasia mutated protein; c-Abl protein; Calcium-Calmodulin-Dependent Protein Kinases - physiology; Cell activation; Cell Cycle - physiology; Cell Differentiation - genetics; Cell fate; Cell Lineage - genetics; Deoxyribonucleic acid; DNA; DNA biosynthesis; DNA damage; DNA Damage - genetics; DNA Damage - physiology; DNA repair; DNA Repair - genetics; DNA-Binding Proteins - physiology; DNA-dependent protein kinase; Enzyme Activation; Genes, Tumor Suppressor; Genotoxicity; Humans; Ionizing radiation; Isoenzymes - physiology; JNK Mitogen-Activated Protein Kinases; Kinases; MAP kinase; Mitogen-Activated Protein Kinases; Nuclear Proteins - physiology; p38 Mitogen-Activated Protein Kinases; p53 Protein; Phosphatidylinositol 3-Kinases - physiology; Phosphorylation; Protein Kinase C - physiology; Protein Kinase C-delta; Protein-tyrosine kinase; Proteins; Proto-Oncogene Proteins c-abl - genetics; Proto-Oncogene Proteins c-abl - metabolism; Proto-Oncogene Proteins c-abl - physiology; Rad51 protein; Recombination; Replication; Stress response; Tumor Protein p73; Tumor Suppressor Proteins

The cellular response to DNA damage includes growth arrest and activation of DNA repair. Certain insights into how DNA damage is converted into intracellular signals that control the genotoxic stress response have been derived from the finding that the c-Abl protein tyrosine kinase is activated by i...