Signaling to p53: breaking the MDM2-p53 circuit
Article Abstract:
The relationship between the p53 tumor suppressor protein and its inhibitor, MDM2, is explained in terms of how MDM2 influences p53 degradation and cellular interaction. The regulation of the MDM2-p53 interaction can either be accomplished by alteration of p53 through covalent modification and production of alternate reading frame (ARF) contained in the p16INK4A locus binded to MDM2. The p53-MDM2 interaction is disrupted upon modification of p53 during a stress stimuli while in the event of an oncogene imbalance, ARF is produced and MDM2 is inhibited from destabilizing p53.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1998
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A role for ATR in the DNA damage-induced phosphorylation of p53
Article Abstract:
A role exists for ATR in DNA-damage-induced phosphorylation of p53. Phosphorylation at Ser-15 may be critical in functional activation of p53 and its up-regulation in cellular stress. Evidence that ATR, ATM-Rad3-related protein, regulates phosphorylation of Ser-15 in DNA-damaged cells exists. It appears that p53 is phosphorylation target for ATR in DNA-damaged cells.
Publication Name: Genes & Development
Subject: Biological sciences
ISSN: 0890-9369
Year: 1999
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DNA damage-induced phosphorylation of p53 alleviates inhibition by MDM2
Article Abstract:
Posttranscriptional mechanisms are used by DNA-damaging agents to signal the protein p53. It is shown that phosphorylation of human p53 at serine 15 occurs following DNA damage, leading to lessened interaction of p53 with the oncoprotein MDM2, its negative regulator. The effects could be due to conformational changes on phosphorylation of p53.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1997
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