Stabilization of p27^Kip1/CDKN1B by UBCH7/UBE2L3 catalyzed ubiquitinylation: a new paradigm in cell-cycle control.

ABSTRACT: Ubiquitinylation drives many cellular processes by targeting proteins for proteasomal degradation. Ubiquitin conjugation enzymes promote ubiquitinylation and, thus, degradation of protein substrates. Ubiquitinylation is a well-known posttranslational modification controlling cell-cycle transitions and levels or/and activation levels of ubiquitin-conjugating enzymes change during development and cell cycle. Progression through the cell cycle is tightly controlled by CDK inhibitors such as p27^Kip1. Here we show that, in contrast to promoting its degradation, the ubiquitin-conjugating enzyme UBCH7/UBE2L3 specifically protects p27^Kip1 from degradation. Overexpression of UBCH7/UBE2L3 stabilizes p27^Kip1 and delays the G₁-to-S transition, while depletio

SUBMITTER: Whitcomb EA 

PROVIDER: S-EPMC6355086 | biostudies-literature | 2019 Jan

REPOSITORIES: biostudies-literature