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Updated: May 13, 2026

Assessment of Mitochondrial Functions and Cell Viability in Renal Cells Overexpressing Protein Kinase C Isozymes
Published on: January 7, 2013
PKCδ enhances C/EBPα degradation via inducing its phosphorylation and cytoplasmic translocation
Zhao-Xia Wu1, Meng Zhao, Li Xia
1The Department of Pathophysiology, Key Laboratory of Cell Differentiation and Apoptosis of Chinese Ministry of Education, Shanghai Jiao-Tong University School of Medicine, Shanghai 200025, China.
Abstract:
Our previous study has shown that PKCδ stimulates proteasome-dependent degradation of C/EBPα, which partially contributes to PKCδ-mediated apoptosis. However, the molecular interrelationship between these two important proteins is still unknown. In this study, we reported that C/EBPα was phosphorylated by activated PKCδ on three serines, two of which were reported for the first time. Phosphorylated C/EBPα underwent cytoplasmic translocation, which led to the inactivation of its transcriptional activity. Inactive cytoplasmic C/EBPα was finally subjected to proteasome degradation. This work reveals the exquisite molecular events linking activated PKCδ and C/EBPα degradation during cell apoptosis.
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