Journal
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume 400, Issue 1, Pages 16-20Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2010.07.126
Keywords
Akt; PKC-alpha; TCR; PDK-2
Categories
Funding
- National Natural Science Foundation of China [30872790/H0908]
- National Institutes of Health (NIH) [R01 AI090901]
- American Heart Association [09GRNT2010084]
- China Scholarship Council of the Ministry of Education of PR China [[2007] 3020]
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Akt signaling plays a central role in T cell functions, such as proliferation, apoptosis, and regulatory T cell development. Phosphorylation at Set(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. (C) 2010 Elsevier Inc. All rights reserved.
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