| First Author | Peng C | Year | 2010 |
| Journal | FASEB J | Volume | 24 |
| Issue | 9 | Pages | 3490-9 |
| PubMed ID | 20385620 | Mgi Jnum | J:163566 |
| Mgi Id | MGI:4822304 | Doi | 10.1096/fj.09-151290 |
| Citation | Peng C, et al. (2010) RSK2 mediates NF-{kappa}B activity through the phosphorylation of IkappaBalpha in the TNF-R1 pathway. FASEB J 24(9):3490-9 |
| abstractText | The ribosomal S6 kinase 2 (RSK2) is a well-known serine/threonine kinase and a member of the p90 ribosomal S6 kinase (p90RSK) family of proteins. It is activated downstream of the MEK/ERKs cascade by mitogenic stimuli such as EGF or TPA. Here, we show that RSK2 is activated by treatment with tumor necrosis factor-alpha (TNF-alpha) and directly phosphorylates IkappaBalpha at Ser-32, leading to IkappaBalpha degradation. The phosphorylation of IkappaBalpha promotes the activation and translocation of the nuclear factor-kappaB (NF-kappaB) subunits p65 and p50 to the nucleus. The net result is an increased NF-kappaB activity, which serves as a mechanism for RSK2 blockade of TNF-alpha-induced apoptosis and enhanced cell survival. |
