Phosphorylation is required for PMA- and cell-cycle-induced degradation of protein kinase Cδ
Copyright policy )Phosphorylation is required for PMA- and cell-cycle-induced degradation of protein kinase Cδ
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 PKCΔ in NIH 3T3 cells under culture conditions where PKCΔ 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 PKCΔ observed on G1/S-phase progression through the cell cycle. Analysis of phosphorylation-site mutants indicated that the T-loop Thr505 phosphorylation site was critical for induced degradation.
- PSL Research University France
- Inserm France
- French National Centre for Scientific Research France
- King's College London United Kingdom
- Center for Interdisciplinary Research in Biology France
Threonine, 570, Ubiquitin, Cell Cycle, 610, Down-Regulation, 3T3 Cells, S Phase, [SDV] Life Sciences [q-bio], Isoenzymes, Mice, Protein Kinase C-delta, [CHIM] Chemical Sciences, Animals, Tetradecanoylphorbol Acetate, Marine Toxins, Phosphorylation, Oxazoles, Protein Kinase C
Threonine, 570, Ubiquitin, Cell Cycle, 610, Down-Regulation, 3T3 Cells, S Phase, [SDV] Life Sciences [q-bio], Isoenzymes, Mice, Protein Kinase C-delta, [CHIM] Chemical Sciences, Animals, Tetradecanoylphorbol Acetate, Marine Toxins, Phosphorylation, Oxazoles, Protein Kinase C
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