| First Author | Niger C | Year | 2010 |
| Journal | BMC Biochem | Volume | 11 |
| Pages | 14 | PubMed ID | 20338032 |
| Mgi Jnum | J:222149 | Mgi Id | MGI:5644021 |
| Doi | 10.1186/1471-2091-11-14 | Citation | Niger C, et al. (2010) Interaction of connexin43 and protein kinase C-delta during FGF2 signaling. BMC Biochem 11:14 |
| abstractText | BACKGROUND: We have recently demonstrated that modulation of the gap junction protein, connexin43, can affect the response of osteoblasts to fibroblast growth factor 2 in a protein kinase C-delta-dependent manner. Others have shown that the C-terminal tail of connexin43 serves as a docking platform for signaling complexes. It is unknown whether protein kinase C-delta can physically interact with connexin43. RESULTS: In the present study, we investigate by immunofluorescent co-detection and biochemical examination the interaction between Cx43 and protein kinase C-delta. We establish that protein kinase C-delta physically interacts with connexin43 during fibroblast growth factor 2 signaling, and that protein kinase C delta preferentially co-precipitates phosphorylated connexin43. Further, we show by pull down assay that protein kinase C-delta associates with the C-terminal tail of connexin43. CONCLUSIONS: Connexin43 can serve as a direct docking platform for the recruitment of protein kinase C-delta in order to affect fibroblast growth factor 2 signaling in osteoblasts. These data expand the list of signal molecules that assemble on the connexin43 C-terminal tail and provide a critical context to understand how gap junctions modify signal transduction cascades in order to impact cell function. |
