Abl tyrosine kinase in signal transduction and cell-cycle regulation

Curr Opin Genet Dev. 1993 Feb;3(1):35-43. doi: 10.1016/s0959-437x(05)80338-7.

Abstract

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.

Publication types

  • Review

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Cell Cycle*
  • Cell Transformation, Neoplastic / genetics
  • Cell Transformation, Neoplastic / metabolism
  • Drosophila melanogaster / enzymology
  • Drosophila melanogaster / genetics
  • Fusion Proteins, bcr-abl / physiology
  • Gene Expression Regulation
  • Genes, abl
  • Mammals / genetics
  • Mammals / metabolism
  • Mice
  • Models, Biological
  • Molecular Sequence Data
  • Multigene Family
  • Oncogene Proteins v-abl / genetics
  • Oncogene Proteins v-abl / physiology
  • Phosphorylation
  • Protein Processing, Post-Translational
  • Protein-Tyrosine Kinases / physiology*
  • Proto-Oncogene Proteins c-abl / physiology*
  • Signal Transduction*
  • Subcellular Fractions / enzymology

Substances

  • Oncogene Proteins v-abl
  • Protein-Tyrosine Kinases
  • Fusion Proteins, bcr-abl
  • Proto-Oncogene Proteins c-abl