PHD3 Regulates p53 Protein Stability by Hydroxylating Proline 359
Abstract
Cellular p53 protein levels are regulated by a ubiquitination/de-ubiquitination cycle that can target the protein for proteasomal destruction. The ubiquitination reaction is catalyzed by a multitude of ligases, whereas the removal of ubiquitin chains is mediated by two deubiquitinating enzymes (DUBs), USP7 (HAUSP) and USP10. Here, we show that PHD3 hydroxylates p53 at proline 359, a residue that is in the p53-DUB binding domain. Hydroxylation of...
Paper Details
Title
PHD3 Regulates p53 Protein Stability by Hydroxylating Proline 359
Published Date
Jul 1, 2018
Journal
Volume
24
Issue
5
Pages
1316 - 1329
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