Abstract
The p27Kip1 cyclin-dependent kinase inhibitor translocates in response to transforming growth factor-β to a Cdk2–cyclin E complex inhibiting its catalytic activity, but the p27Kip1 protein levels are unaffected [1]. We show here that transforming growth factor-β induces the accumulation of a form of p27Kip1 representing a subpopulation of total p27Kip1 in growth-arrested Mv1Lu epithelial cells. The inducible p27Kip1 is detectable only by a specific p27Kip1 monoclonal antibody recognizing a native form of p27Kip1. The increase in this subset of p27Kip1 correlates with G1 arrest and withdrawal of the cells from the cycle induced by transforming growth factor-β, serum starvation, or contact inhibition. In contrast to the majority of p27Kip1 in the cells, the transforming growth factor-β-inducible p27Kip1 is devoid of cyclin-dependent kinase/cyclin interactions. The results indicate that growth arresting treatments induce the accumulation of non-cyclin-dependent kinase-bound p27Kip1, which may function as a reservoir for inhibition of Cdk2–cyclin E activities.
Published Version
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