| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1928733 | Biochemical and Biophysical Research Communications | 2013 | 6 Pages |
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.
Graphical abstractFigure optionsDownload full-size imageDownload as PowerPoint slideHighlights► Activated PKCδ stimulates cytoplasmic translocation of C/EBPα protein. ► Activated PKCδ enhances phosphorylation of C/EBPα. ► Two new phosphosites of C/EBPα have been identified.
