Abstract
The proto-oncogene c- abl encodes a protein tyrosine kinase that is localized in the cytoplasm and the nucleus. The large carboxyl-terminal segment of c-Abl was found to contain a DNA-binding domain that was necessary for the association of c-Abl with chromatin. The DNA-binding activity of c-Abl was lost during mitosis when the carboxyl-terminal segment became phosphorylated. In vitro phosphorylation of the DNA-binding domain by cdc2 kinase abolished DNA binding. Homozygous mutant mice expressing a c-Abl tyrosine kinase without the DNA-binding domain have been reported to die of multiple defects at birth. Thus, binding of the c-Abl tyrosine kinase to DNA may be essential to its biological function.
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Dates
Type | When |
---|---|
Created | 18 years, 10 months ago (Oct. 5, 2006, 7:03 p.m.) |
Deposited | 1 year, 7 months ago (Jan. 12, 2024, 6:32 p.m.) |
Indexed | 3 months, 2 weeks ago (May 5, 2025, 5:02 a.m.) |
Issued | 33 years, 4 months ago (April 17, 1992) |
Published | 33 years, 4 months ago (April 17, 1992) |
Published Print | 33 years, 4 months ago (April 17, 1992) |
@article{Kipreos_1992, title={Cell Cycle—Regulated Binding of c-Abl Tyrosine Kinase to DNA}, volume={256}, ISSN={1095-9203}, url={http://dx.doi.org/10.1126/science.256.5055.382}, DOI={10.1126/science.256.5055.382}, number={5055}, journal={Science}, publisher={American Association for the Advancement of Science (AAAS)}, author={Kipreos, Edward T. and Wang, Jean Y. J.}, year={1992}, month=apr, pages={382–385} }