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PML tumor suppressor is regulated by HIPK2-mediated phosphorylation in response to DNA damage.

Oncogene | Feb 5, 2009

http://www.ncbi.nlm.nih.gov/pubmed/19015637

The promyelocytic leukemia (PML) tumor suppressor protein, a central regulator of cell proliferation and apoptosis, is frequently fused to the retinoic acid receptor-alpha (RARalpha) in acute PML. Here we show the interaction of PML with another tumor suppressor protein, the serine/threonine kinase homeodomain-interacting protein kinase (HIPK2). In response to DNA damage, HIPK2 phosphorylates PML at serines 8 and 38. Although HIPK2-mediated phosphorylation of PML occurs early during the DNA damage response, the oncogenic PML-RARalpha fusion protein is phosphorylated with significantly delayed kinetics. DNA damage or HIPK2 expression leads to the stabilization of PML and PML-RARalpha proteins. The N-terminal phosphorylation sites contribute to the DNA damage-induced PML SUMOylation and are required for the ability of PML to cooperate with HIPK2 for the induction of cell death.

Pubmed ID: 19015637 RIS Download

Mesh terms: Carrier Proteins | Cell Death | Cells, Cultured | DNA Damage | Genes, Tumor Suppressor | Humans | Nuclear Proteins | Phosphorylation | Protein Binding | Protein Processing, Post-Translational | Protein Stability | Protein Structure, Tertiary | Protein-Serine-Threonine Kinases | SUMO-1 Protein | Serine | Transcription Factors | Tumor Suppressor Proteins

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