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A C-terminal protein-binding domain in the retinoblastoma protein regulates nuclear c-Abl tyrosine kinase in the cell cycle.

Cell | Nov 19, 1993

http://www.ncbi.nlm.nih.gov/pubmed/8242749

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.

Pubmed ID: 8242749 RIS Download

Mesh terms: Adenosine Triphosphate | Amino Acid Sequence | Binding Sites | Cell Cycle | Cell Nucleus | Enzyme Activation | Growth Inhibitors | Growth Substances | Humans | In Vitro Techniques | Molecular Sequence Data | Nuclear Proteins | Oligopeptides | Phosphorylation | Precipitin Tests | Protein Binding | Protein-Tyrosine Kinases | Proto-Oncogene Proteins c-abl | Retinoblastoma Protein | S Phase | Trans-Activators | Tumor Cells, Cultured

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