Repression of the CDK activator Cdc25A and cell-cycle arrest by cytokine TGF-β in cells lacking the CDK inhibitor p15 View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1997-05

AUTHORS

A Iavarone, J Massagué

ABSTRACT

The activity of the cyclin-dependent kinases (CDKs) that control cell growth and division can be negatively regulated by tyrosine phosphorylation or by the binding of various CDK inhibitors. Whereas regulation by tyrosine phosphorylation is well documented in CDKs that function during mitosis, little is known about its role in the regulation of CDKs that act in the G1 phase of the cell cycle. In contrast, much evidence has accumulated on the regulation of G1 CDKs by CDK inhibitors. The cytokine TGF-beta inhibits growth by causing cell-cycle arrest as a result of increasing the concentration of the Cdk4/6 inhibitor p15(INK4B/MTS2) (refs 3, 4). Here we report that TGF-beta can also cause the inhibition of Cdk4 and Cdk6 by increasing their level of tyrosine phosphorylation. Tyrosine phosphorylation and inactivation of Cdk4/6 in a human mammary epithelial cell line are shown to result from the ability of TGF-beta to repress expression of the CDK tyrosine phosphatase Cdc25A. Repression of Cdc25A and induction of p15 are independent effects mediating the inhibition of Cdk4/6 by TFG-beta. More... »

PAGES

417-422

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/387417a0

DOI

http://dx.doi.org/10.1038/387417a0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1011555947

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/9163429


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