| First Author | Shi J | Year | 2012 |
| Journal | FEBS Lett | Volume | 586 |
| Issue | 16 | Pages | 2443-50 |
| PubMed ID | 22687243 | Mgi Jnum | J:186998 |
| Mgi Id | MGI:5435106 | Doi | 10.1016/j.febslet.2012.05.063 |
| Citation | Shi J, et al. (2012) Diverse regulation of AKT and GSK-3beta by O-GlcNAcylation in various types of cells. FEBS Lett 586(16):2443-50 |
| abstractText | Protein kinase B (AKT) and glycogen synthase kinase-3beta (GSK-3beta) are major components of insulin-AKT signaling that plays crucial roles in various types of tissue. Recent studies found that these two kinases are modified posttranslationally by O-GlcNAcylation. Here, we demonstrate that O-GlcNAcylation regulated phosphorylation/activation of AKT and GSK-3beta in different manners in kidney HEK-293FT cells, but did not affect these two kinases in hepatic HepG2 cells. In neuronal cells, O-GlcNAcylation regulated phosphorylation of AKT negatively, but had no effect on GSK-3beta. These results suggest protein-specific and cell type-specific regulation of AKT and GSK-3beta by O-GlcNAcylation. Therefore, studies on the roles of AKT and GSK-3beta O-GlcNAcylation should be done in a tissue- and cell type-specific manner. |
