Ontology highlight
ABSTRACT:
SUBMITTER: Podust VN
PROVIDER: S-EPMC18275 | biostudies-literature | 2000 Apr
REPOSITORIES: biostudies-literature
Podust V N VN Brownell J E JE Gladysheva T B TB Luo R S RS Wang C C Coggins M B MB Pierce J W JW Lightcap E S ES Chau V V
Proceedings of the National Academy of Sciences of the United States of America 20000401 9
Temporal control of p27(Kip1) (p27) degradation imposes periodicity in its activity during cell cycle progression and its accumulation during cell cycle exit. Degradation of p27 is initiated by phosphorylation of p27 at Thr-187, which marks the protein for ubiquitination by SCF(Skp2) and subsequent proteolysis by the 26S proteasome. Here we show that the p27 ubiquitination activity in cell extracts depends on the presence of the ubiquitin-like protein Nedd8 and enzymes that catalyze Nedd8 conjug ...[more]