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- Title
Tumour suppression: Disruption of HAUSP gene stabilizes p53.
- Authors
Cummins, Jordan M.; Rago, Carlo; Kohli, Manu; Kinzler, Kenneth W.; Lengauer, Christoph; Vogelstein, Bert
- Abstract
Ubiquitination of p53 is the principal echanism through which p53 concentrations in the cell are regulated in order to maintain its effects on tumorienesis and normal cell growth. The protein HAUSP is a ubiquitinspecific protease. The absence of HAUSP protein in the knockout clones was confirmed by western blotting. Surprisingly, the absence of HAUSP resulted in a substantial increase in the steady-state level of p53 protein. To test the generality of these results, researchers attempted to disrupt the HAUSP gene in two other lines with intact p53 function, one derived from a cancer cell line and the other derived from telomerase-immortalizcd, normal retinal-pigment epithelial cells.
- Subjects
PROTEOLYTIC enzymes; GROWTH factors; PROTEINS; EPITHELIAL cells; CANCER cells; EPITHELIUM
- Publication
Nature, 2004, Vol 428, Issue 6982, p1
- ISSN
0028-0836
- Publication type
Article
- DOI
10.1038/nature02501