PML interaction with p53 and its role in apoptosis and replicative senescence.
A network of control pathways has been characterized that arrest growth or induce apoptosis in response to potentially tumorogenic events such as genotoxic stress or oncogene expression. Ablation, or functional disruption, of these pathways is frequently observed during multistep carcinogenesis. Analysis of those genes most commonly compromized in tumours has led to the identification of the transcription factor p53 and the E2F binding protein Retinoblastoma (Rb), as key regulators of these processes. This review discusses recent data, demonstrating that the Promyelocytic Leukemia (PML) protein can physically and functionally interact with both p53 and Rb, suggesting that PML may be a novel regulator of these pathways.
Pearson
M
M
Department of Experimental Oncology, European Institute of Oncology, Milano 20141, Italy. mark.pearson@ieo.it
Pelicci
P G
PG
D000123:Acetyltransferases / Q000378:metabolism; D048868:Adaptor Proteins, Signal Transducing; D000818:Animals; D017209:Apoptosis / Q000502:physiology*; D002352:Carrier Proteins / Q000378:metabolism; D022003:Cell Nucleus Structures / Q000378:metabolism; D016922:Cellular Senescence / Q000502:physiology*; D056970:Co-Repressor Proteins; D051548:Histone Acetyltransferases; D006801:Humans; D047908:Intracellular Signaling Peptides and Proteins; D018832:Molecular Chaperones; D009363:Neoplasm Proteins / Q000378:metabolism*; D009687:Nuclear Proteins; D000071156:Promyelocytic Leukemia Protein; D011485:Protein Binding / Q000502:physiology; D016160:Retinoblastoma Protein / Q000378:metabolism*; D029701:Saccharomyces cerevisiae Proteins; D013312:Stress, Physiological / Q000378:metabolism; D014157:Transcription Factors / Q000378:metabolism*; D016159:Tumor Suppressor Protein p53 / Q000378:metabolism*; D025521:Tumor Suppressor Proteins
D048868:Adaptor Proteins, Signal Transducing; D002352:Carrier Proteins; D056970:Co-Repressor Proteins; C106985:DAXX protein, human; D047908:Intracellular Signaling Peptides and Proteins; D018832:Molecular Chaperones; D009363:Neoplasm Proteins; D009687:Nuclear Proteins; D000071156:Promyelocytic Leukemia Protein; D016160:Retinoblastoma Protein; D029701:Saccharomyces cerevisiae Proteins; D014157:Transcription Factors; D016159:Tumor Suppressor Protein p53; D025521:Tumor Suppressor Proteins; C070576:PML protein, human; D000123:Acetyltransferases; D051548:Histone Acetyltransferases