Open AccessA cell cycle-regulated inhibitor of cyclin-dependent kinases.
Author(s) -
Ludger Hengst,
Vjekoslav Dulić,
Joyce M. Slingerland,
Emma Lees,
Steven I. Reed
Publication year - 1994
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.91.12.5291
Subject(s) - cyclin dependent kinase , kinase , cell cycle , microbiology and biotechnology , cdk inhibitor , cyclin , cyclin dependent kinase complex , restriction point , cyclin a , cyclin dependent kinase 3 , biology , cyclin d , cyclin dependent kinase 2 , cyclin dependent kinase 4 , polo like kinase , biochemistry , chemistry , cell , protein kinase a
Cyclin-dependent kinases (Cdks) previously have been shown to drive the major cell cycle transitions in eukaryotic organisms ranging from yeast to humans. We report here the identification of a 28-kDa protein, p28Ick (inhibitor of cyclin-dependent kinase), that binds to and inhibits the kinase activity of preformed Cdk/cyclin complexes from human cells. p28 inhibitory activity fluctuates during the cell cycle with maximal levels in G1 and accumulates in G1- and G0-arrested cells. These results suggest that control of the G1/S transition may be influenced by a family of Cdk inhibitors that include p28Ick and the recently described inhibitors p21Cip1/Waf1/Cap20 and p16Ink4.