CK2 and PML: Regulating the Regulator
Copyright policy )CK2 and PML: Regulating the Regulator
The PML protein induces senescence, and, upon oncogenic stress, its absence promotes cellular transformation. In this issue of Cell, Scaglioni et al. (2006) show that phosphorylation of PML by CK2, a kinase frequently activated in human cancers, promotes PML degradation. Therefore, pharmacological inhibition of CK2-induced PML loss could be used to offset tumor establishment.
- UNIVERSITE PARIS DESCARTES France
- French National Centre for Scientific Research France
- Assistance Publique -Hopitaux De Paris France
- University of Paris France
- Inserm France
Proteasome Endopeptidase Complex, Lung Neoplasms, Biochemistry, Genetics and Molecular Biology(all), Tumor Suppressor Proteins, Nuclear Proteins, Promyelocytic Leukemia Protein, Neoplasm Proteins, Enzyme Activation, Gene Expression Regulation, Neoplastic, Cell Transformation, Neoplastic, Carcinoma, Non-Small-Cell Lung, Humans, Genes, Tumor Suppressor, Phosphorylation, Casein Kinase II, Transcription Factors
Proteasome Endopeptidase Complex, Lung Neoplasms, Biochemistry, Genetics and Molecular Biology(all), Tumor Suppressor Proteins, Nuclear Proteins, Promyelocytic Leukemia Protein, Neoplasm Proteins, Enzyme Activation, Gene Expression Regulation, Neoplastic, Cell Transformation, Neoplastic, Carcinoma, Non-Small-Cell Lung, Humans, Genes, Tumor Suppressor, Phosphorylation, Casein Kinase II, Transcription Factors
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