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Biochem J. 2002 Nov 15;368(Pt 1):349-55.

Phosphorylation is required for PMA- and cell-cycle-induced degradation of protein kinase Cdelta.

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Protein Phosphorylation Laboratory, Cancer Research UK London Institute, Lincoln's Inn Fields Laboratories, 44 Lincoln's Inn Fields, London WC2A 3PX, U.K.


Classical and novel protein kinase C (PKC) isoforms are down-regulated as a result of chronic activation by certain tumour promoters and physiological stimuli; however, the mechanisms leading to down-regulation are not fully understood. In the present study, we have studied the PMA ('TPA')-induced degradation of PKCdelta in NIH 3T3 cells under culture conditions where PKCdelta displays cell-cycle-dependent down-regulation. In contrast with previous studies, a hyperphosphorylated form of this PKC isoform, promoted by calyculin A, was rapidly degraded in PMA-treated cells. Similarly, the presence of calyculin A enhanced the down-regulation of PKCdelta observed on G(1)/S-phase progression through the cell cycle. Analysis of phosphorylation-site mutants indicated that the T-loop Thr(505) phosphorylation site was critical for induced degradation.

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