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. 1994 Mar;14(3):1997-2003.
doi: 10.1128/mcb.14.3.1997-2003.1994.

Accumulation of p53 in a mutant cell line defective in the ubiquitin pathway

D R Chowdary  1 , J J Dermody, K K Jha, H L Ozer
Affiliations

Accumulation of p53 in a mutant cell line defective in the ubiquitin pathway

D R Chowdary et al. Mol Cell Biol. 1994 Mar.

Abstract

The wild-type p53 gene product plays an important role in the control of cell proliferation, differentiation, and survival. Altered function is frequently associated with changes in p53 stability. We have studied the role of the ubiquitination pathway in the degradation of p53, utilizing a temperature-sensitive mutant, ts20, derived from the mouse cell line BALB/c 3T3. We found that wild-type p53 accumulates markedly because of decreased breakdown when cells are shifted to the restrictive temperature. Introduction of sequences encoding the human ubiquitin-activating enzyme E1 corrects the temperature sensitivity defect in ts20 and prevents accumulation of p53. The data therefore strongly indicate that wild-type p53 is degraded intracellularly by the ubiquitin-mediated proteolytic pathway.

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