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Vorinostat is a histone deacetylase inhibitor that blocks cancer cell proliferationthrough the regulation of cyclin-dependent kinase inhibitors. We, herein, examinedthe involvement of S-phase kinase-associated protein 2 (Skp2) and cyclin-dependentkinase subunit 1 (Cks1), the components of the SCFSkp2-Cks1 (Skp1/Cul1/F-box protein)ubiquitin ligase complex, in the regulation of p27 and p21 during vorinostat-inducedgrowth arrest of MDA-MB-231 and MCF-7 human breast cancer cells. Vorinostat significantlyreduced BrdU incorporation in MDA-MB-231 and MCF-7 cells, which was associatedwith increased p27 and p21 protein levels without concomitant induction of p27mRNA. Vorinostat-induced accumulation of p27 and p21 proteins was inversely correlatedwith the mRNA and protein levels of Skp2 and Cks1. Cycloheximide chase analysisrevealed that vorinostat increased the half-life of p27 and p21 proteins. Theaccumulation of p27 and p21 proteins was attenuated by forced expression of Skp2and Cks1, which conferred resistance to the vorinostat-induced S-phase reduction.These results suggest that vorinostat-induced growth arrest may be in part dueto the enhanced protein stability of p27 and p21 through the downregulation ofSkp2 and Cks1.

Vorinostat enhances protein stability of p27 and p21 through negative regulation of Skp2 and Cks1 in human breast cancer cells