| First Author | Xu Y | Year | 2015 |
| Journal | Biochim Biophys Acta | Volume | 1850 |
| Issue | 12 | Pages | 2552-62 |
| PubMed ID | 26367078 | Mgi Jnum | J:254549 |
| Mgi Id | MGI:6100443 | Doi | 10.1016/j.bbagen.2015.09.008 |
| Citation | Xu Y, et al. (2015) Cidec promotes the differentiation of human adipocytes by degradation of AMPKalpha through ubiquitin-proteasome pathway. Biochim Biophys Acta 1850(12):2552-62 |
| abstractText | BACKGROUND: We previously showed that Cidec was localized on the surface of lipid droplets and could promote the differentiation of human adipocytes, but the molecular mechanism was still unknown. METHODS & RESULTS: In this study, we first sought to identify proteins that interact with Cidec using yeast two-hybrid system. The results revealed that Cidec could directly interact with AMPKalpha1 subunit. We further showed that AMPKalpha levels decreased while Cidec increased during the adipogenic differentiation of human adipocytes. Meanwhile, we observed that the increased Cidec could reduce AMPKalpha level in adipocytes, and the downregulation of AMPKalpha could help to promote the differentiation of adipocytes. The results of co-immunoprecipitation and immunofluorescent proved that Cidec biochemically interacted and co-localized with AMPKalpha1, which meant Cidec was a regulator for AMPKalpha stability through an ubiquitin-proteasome pathway. CONCLUSION: Our data suggested that Cidec could interact with and down-regulate AMPKalpha through an ubiquitin-proteasome degradation pathway, which provided a possible mechanism of Cidec in promoting human adipocytes differentiation. GENERAL SIGNIFICANCE: Our work proposed a new possible mechanism for human adipogenesis, and also provided a potential role of AMPKalpha as a target in treating obesity or obesity-related diseases. |
