Abl tyrosine kinase in signal transduction and cell-cycle regulation.
Although the biological function of the c-Abl tyrosine kinase remains unsolved, potentially productive avenues towards the elucidation of that function have been identified by recent progress. An F-actin binding and a sequence-specific DNA-binding domain have been discovered in c-Abl, and DNA binding has been shown to be cell-cycle regulated. Deletion of those two domains in the mouse c-Abl results in a loss of biological function despite the production of an active tyrosine kinase. These findings suggest a role for c-Abl in the regulation of processes occurring on F-actin and on specific DNA elements.
Wang
J Y
JY
Department of Biology and Center for Molecular Genetics, University of California, San Diego 92093-0116.
D000595:Amino Acid Sequence; D000818:Animals; D002453:Cell Cycle; D002471:Cell Transformation, Neoplastic / Q000235:genetics / Q000378:metabolism; D004331:Drosophila melanogaster / Q000201:enzymology / Q000235:genetics; D016044:Fusion Proteins, bcr-abl / Q000502:physiology; D005786:Gene Expression Regulation; D016313:Genes, abl; D008322:Mammals / Q000235:genetics / Q000378:metabolism; D051379:Mice; D008954:Models, Biological; D008969:Molecular Sequence Data; D005810:Multigene Family; D016374:Oncogene Proteins v-abl / Q000235:genetics / Q000502:physiology; D010766:Phosphorylation; D011499:Protein Processing, Post-Translational; D011505:Protein-Tyrosine Kinases / Q000502:physiology*; D016315:Proto-Oncogene Proteins c-abl / Q000502:physiology*; D015398:Signal Transduction; D013347:Subcellular Fractions / Q000201:enzymology
D016374:Oncogene Proteins v-abl; D011505:Protein-Tyrosine Kinases; D016044:Fusion Proteins, bcr-abl; D016315:Proto-Oncogene Proteins c-abl