期刊
MOLECULAR CELL
卷 5, 期 2, 页码 403-410出版社
CELL PRESS
DOI: 10.1016/S1097-2765(00)80435-9
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资金
- NCI NIH HHS [CA6421] Funding Source: Medline
The Cdk inhibitor p21(Cip1) is an unstable protein. Pharmacologic inhibition of the proteasome increases the half-life of p21 from less than 30 min to more than 2 hr and results in the accumulation of p21-ubiquitin conjugates. To determine whether ubiquitination was required for proteasomal degradation of p21, we constructed mutant versions of p21 that were not ubiquitinated in vivo. Remarkably, these mutants remained unstable and increased in abundance upon proteasome inhibition, indicating that direct ubiquitination of p21 is not necessary for its turnover by the proteasome. The frequently observed correlation between protein ubiquitination and proteasomal degradation is insufficient to conclude that ubiquitination is a prerequisite for degradation.
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