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PML interaction with p53 and its role in apoptosis and replicative senescence Pearson M; Pelicci PGOncogene 2001[Oct]; 20 (49): 7250-6A 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.|*Intracellular Signaling Peptides and Proteins[MESH]|*Nuclear Proteins[MESH]|*Saccharomyces cerevisiae Proteins[MESH]|Acetyltransferases/metabolism[MESH]|Adaptor Proteins, Signal Transducing[MESH]|Animals[MESH]|Apoptosis/*physiology[MESH]|Carrier Proteins/metabolism[MESH]|Cell Nucleus Structures/metabolism[MESH]|Cellular Senescence/*physiology[MESH]|Co-Repressor Proteins[MESH]|Histone Acetyltransferases[MESH]|Humans[MESH]|Molecular Chaperones[MESH]|Neoplasm Proteins/*metabolism[MESH]|Promyelocytic Leukemia Protein[MESH]|Protein Binding/physiology[MESH]|Retinoblastoma Protein/*metabolism[MESH]|Stress, Physiological/metabolism[MESH]|Transcription Factors/*metabolism[MESH]|Tumor Suppressor Protein p53/*metabolism[MESH]|Tumor Suppressor Proteins[MESH] |
