Abstract
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.
MeSH terms
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Carcinoma, Non-Small-Cell Lung / enzymology
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Carcinoma, Non-Small-Cell Lung / genetics
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Carcinoma, Non-Small-Cell Lung / pathology
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Casein Kinase II / antagonists & inhibitors
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Casein Kinase II / genetics
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Casein Kinase II / metabolism*
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Cell Transformation, Neoplastic
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Enzyme Activation
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Gene Expression Regulation, Neoplastic*
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Genes, Tumor Suppressor*
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Humans
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Lung Neoplasms / enzymology
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Lung Neoplasms / genetics
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Lung Neoplasms / pathology
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Neoplasm Proteins / antagonists & inhibitors
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Neoplasm Proteins / chemistry
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Neoplasm Proteins / genetics
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Neoplasm Proteins / metabolism*
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Neoplasm Proteins / physiology
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Nuclear Proteins / antagonists & inhibitors
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Nuclear Proteins / chemistry
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Nuclear Proteins / genetics
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Nuclear Proteins / metabolism*
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Nuclear Proteins / physiology
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Phosphorylation
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Promyelocytic Leukemia Protein
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Proteasome Endopeptidase Complex / metabolism
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Transcription Factors / antagonists & inhibitors
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Transcription Factors / chemistry
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Transcription Factors / genetics
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Transcription Factors / metabolism*
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Transcription Factors / physiology
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Tumor Suppressor Proteins / antagonists & inhibitors
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Tumor Suppressor Proteins / chemistry
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Tumor Suppressor Proteins / genetics
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Tumor Suppressor Proteins / metabolism*
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Tumor Suppressor Proteins / physiology
Substances
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Neoplasm Proteins
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Nuclear Proteins
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Promyelocytic Leukemia Protein
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Transcription Factors
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Tumor Suppressor Proteins
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PML protein, human
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Casein Kinase II
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Proteasome Endopeptidase Complex