Cell-cycle inhibition by independent CDK and PCNA binding domains in p21Cip1 View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1995-05

AUTHORS

Yan Luo, Jerard Hurwitz, Joan Massagué

ABSTRACT

MAMMALIAN cell-cycle control by antimitogenic signals involves p21Cip1/WAF1(refs 1–4), p27Kip1 (refs 5,6) andp57Kip2(refs 7,8) a family of proteins that bind to and inhibit cyclin-dependent kinases (CDKs) required for initiation of S phase. The protein p21 also binds to the DNA polymerase δ processivity factor, proliferating-cell nuclear antigen (PCNA), and inhibits in vitro PCNA-dependent DNA replication9,10. The CDK and PCNA inhibitory activities of p21 are shown here to be functionally independent and to reside in separate protein domains. The PCNA binding and inhibitory activities, which are not observed with p27 or p57, reside in the C-terminal domain of p21, whereas the CDK inhibitory activity resides in the conserved N-terminal domains of these proteins. When separately overexpressed in mammalian cells, the CDK and PCNA inhibitory domains prevent DNA replication, demonstrating a dual function of p21 as a cell-cycle inhibitor in vivo. More... »

PAGES

159-161

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/375159a0

DOI

http://dx.doi.org/10.1038/375159a0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1011778830

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/7753174


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