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Titolo:
INHIBITION OF CYCLIN-DEPENDENT KINASES BY P21
Autore:
HARPER JW; ELLEDGE SJ; KEYOMARSI K; DYNLACHT B; TSAI LH; ZHANG PM; DOBROWOLSKI S; BAI C; CONNELLCROWLEY L; SWINDELL E; FOX MP; WEI N;
Indirizzi:
BAYLOR COLL MED,DEPT BIOCHEM,ONE BAYLOR PLAZA HOUSTON TX 77030 BAYLOR COLL MED,VERNA & MARRS MCLEAN DEPT BIOCHEM HOUSTON TX 77030 BAYLOR COLL MED,DEPT MOLEC & HUMAN GENET HOUSTON TX 77030 BAYLOR COLL MED,HOWARD HUGHES MED INST HOUSTON TX 77030 MASSACHUSETTS GEN HOSP,CTR CANC,MOLEC ONCOL LAB BOSTON MA 02129 NEW YORK STATE DEPT HLTH,WADSWORTH CTR LABS & RES ALBANY NY 12201
Titolo Testata:
Molecular biology of the cell
fascicolo: 4, volume: 6, anno: 1995,
pagine: 387 - 400
SICI:
1059-1524(1995)6:4<387:IOCKBP>2.0.ZU;2-7
Fonte:
ISI
Lingua:
ENG
Soggetto:
CELL-CYCLE; RETINOBLASTOMA PROTEIN; SUBUNIT;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
38
Recensione:
Indirizzi per estratti:
Citazione:
J.W. Harper et al., "INHIBITION OF CYCLIN-DEPENDENT KINASES BY P21", Molecular biology of the cell, 6(4), 1995, pp. 387-400

Abstract

p21(Cip1) is a cyclin-dependent kinase (Cdk) inhibitor that is transcriptionally activated by p53 in response to DNA damage. We have explored the interaction of p21 with the currently known Cdks. p21 effectively inhibits Cdk2, Cdk3, Cdk4, and Cdk6 kinases (K-i 0.5-15 nM) but is much less effective toward Cdc2/cyclin B (K-i similar to 400 nM) and Cdk5/p35 (K-i > 2 mu M), and does not associate with Cdk7/cyclin H. Overexpression of p21 arrests cells in G1. Thus, p21 is not a universal inhibitor of Cdks but displays selectivity for G1/S Cdk/cyclin complexes. Association of p21 with Cdks is greatly enhanced by cyclin binding. This property is shared by the structurally related inhibitor p27, suggesting a common biochemical mechanism for inhibition. With respect to Cdk2 and Cdk4 complexes, p27 shares the inhibitory potency of p21 but has slightly different kinase specificities. In normal diploid fibroblasts, the vast majority of active Cdk2 is associated with p21, but this active kinase can be fully inhibited by addition of exogenous p21. Reconstruction experiments using purified components indicate that multiple molecules of p21 can associate with Cdk/cyclin complexes and inactive complexes contain more than one molecule of p21. Together, these data suggest a model whereby p21 functions as an inhibitory buffer whose levels determine the threshold kinase activity required for cell cycle progression.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 02/12/20 alle ore 15:16:25