| First Author | Yang L | Year | 2010 |
| Journal | Biochem Biophys Res Commun | Volume | 400 |
| Issue | 1 | Pages | 16-20 |
| PubMed ID | 20691662 | Mgi Jnum | J:164802 |
| Mgi Id | MGI:4835345 | Doi | 10.1016/j.bbrc.2010.07.126 |
| Citation | Yang L, et al. (2010) TCR-induced Akt serine 473 phosphorylation is regulated by protein kinase C-alpha. Biochem Biophys Res Commun 400(1):16-20 |
| abstractText | Akt signaling plays a central role in T cell functions, such as proliferation, apoptosis, and regulatory T cell development. Phosphorylation at Ser(473) in the hydrophobic motif, along with Thr(308) in its activation loop, is considered necessary for Akt function. It is widely accepted that phosphoinositide-dependent kinase 1 (PDK-1) phosphorylates Akt at Thr(308), but the kinase(s) responsible for phosphorylating Akt at Ser(473) (PDK-2) remains elusive. The existence of PDK-2 is considered to be specific to cell type and stimulus. PDK-2 in T cells in response to TCR stimulation has not been clearly defined. In this study, we found that conventional PKC positively regulated TCR-induced Akt Ser(473) phosphorylation. PKC-alpha purified from T cells can phosphorylate Akt at Ser(473) in vitro upon TCR stimulation. Knockdown of PKC-alpha in T-cell-line Jurkat cells reduced TCR-induced phosphorylation of Akt as well as its downstream targets. Thus our results suggest that PKC-alpha is a candidate for PDK-2 in T cells upon TCR stimulation. |
