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rdf:type |
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lifeskim:mentions |
umls-concept:C0007586,
umls-concept:C0007634,
umls-concept:C0033681,
umls-concept:C0080113,
umls-concept:C0521447,
umls-concept:C0851285,
umls-concept:C1514562,
umls-concept:C1704928,
umls-concept:C1707271,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221
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pubmed:issue |
4
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pubmed:dateCreated |
1993-12-29
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pubmed:abstractText |
The ubiquitously expressed c-Abl tyrosine kinase is localized to the nucleus and binds to DNA. The DNA binding activity is regulated by cdc2-mediated phosphorylation, suggesting a cell cycle function for c-Abl. Here we show that the tyrosine kinase activity of nuclear c-Abl is regulated in the cell cycle through a specific interaction with the retinoblastoma protein (RB). A domain in the C-terminus of RB, outside of the A/B pocket, binds to the ATP-binding lobe of the c-Abl tyrosine kinase, resulting in kinase inhibition. The RB-c-Abl interaction is not affected by the viral oncoproteins that bind to RB. Hyperphosphorylation of RB correlates with release of c-Abl and activation of the tyrosine kinase in S phase cells. The nuclear c-Abl tyrosine kinase can enhance transcription, and this activity is inhibited by RB. Nuclear c-Abl is an S phase-activated tyrosine kinase that may participate directly in the regulation of transcription.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0092-8674
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
19
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pubmed:volume |
75
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pubmed:geneSymbol |
RB1,
c-abl
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
779-90
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:8242749-Adenosine Triphosphate,
pubmed-meshheading:8242749-Amino Acid Sequence,
pubmed-meshheading:8242749-Binding Sites,
pubmed-meshheading:8242749-Cell Cycle,
pubmed-meshheading:8242749-Cell Nucleus,
pubmed-meshheading:8242749-Enzyme Activation,
pubmed-meshheading:8242749-Growth Inhibitors,
pubmed-meshheading:8242749-Growth Substances,
pubmed-meshheading:8242749-Humans,
pubmed-meshheading:8242749-Molecular Sequence Data,
pubmed-meshheading:8242749-Nuclear Proteins,
pubmed-meshheading:8242749-Oligopeptides,
pubmed-meshheading:8242749-Phosphorylation,
pubmed-meshheading:8242749-Precipitin Tests,
pubmed-meshheading:8242749-Protein Binding,
pubmed-meshheading:8242749-Protein-Tyrosine Kinases,
pubmed-meshheading:8242749-Proto-Oncogene Proteins c-abl,
pubmed-meshheading:8242749-Retinoblastoma Protein,
pubmed-meshheading:8242749-S Phase,
pubmed-meshheading:8242749-Trans-Activators,
pubmed-meshheading:8242749-Tumor Cells, Cultured
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pubmed:year |
1993
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pubmed:articleTitle |
A C-terminal protein-binding domain in the retinoblastoma protein regulates nuclear c-Abl tyrosine kinase in the cell cycle.
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pubmed:affiliation |
Department of Biology, University of California, San Diego, La Jolla 92093-0116.
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pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, U.S. Gov't, P.H.S.
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