TCR-induced Akt serine 473 phosphorylation is regulated by protein kinase C-alpha

Lifen Yang; Guilin Qiao; Haiyan Ying; Jian Zhang; Fei Yin

doi:10.1016/j.bbrc.2010.07.126

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TCR-induced Akt serine 473 phosphorylation is regulated by protein kinase C-alpha

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TCR-induced Akt serine 473 phosphorylation is regulated by protein kinase C-alpha

Lifen Yang, Guilin Qiao, Haiyan Ying, Jian Zhang and Fei Yin

Biochemical and biophysical research communications, Vol.400(1), pp.16-20

2010

DOI: 10.1016/j.bbrc.2010.07.126

PMCID: PMC2943231

PMID: 20691662

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https://www.ncbi.nlm.nih.gov/pmc/articles/2943231View

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Abstract

► Conventional PKC positively regulates TCR-induced phosphorylation of Akt. ► PKC-alpha is the PDK-2 responsible for phosphorylating Akt at Ser 473 upon TCR stimulation. ► Knockdown of PKC-alpha decreases TCR-induced Akt phosphorylation. 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.

PKC-alpha

TCR

Akt

PDK-2

Details

Title: Subtitle: TCR-induced Akt serine 473 phosphorylation is regulated by protein kinase C-alpha
Creators: Lifen Yang - Department of Pediatrics, Xiangya Hospital, Central South University, Changsha, Hunan, PR China
Guilin Qiao - Section of Nephrology, Department of Medicine, The University of Chicago, Chicago, IL 60637, USA
Haiyan Ying - Section of Nephrology, Department of Medicine, The University of Chicago, Chicago, IL 60637, USA
Jian Zhang - Department of Pediatrics, Xiangya Hospital, Central South University, Changsha, Hunan, PR China
Fei Yin - Department of Pediatrics, Xiangya Hospital, Central South University, Changsha, Hunan, PR China
Resource Type: Journal article
Publication Details: Biochemical and biophysical research communications, Vol.400(1), pp.16-20
DOI: 10.1016/j.bbrc.2010.07.126
PMID: 20691662
PMCID: PMC2943231
NLM abbreviation: Biochem Biophys Res Commun
ISSN: 0006-291X
eISSN: 1090-2104
Publisher: Elsevier Inc
Grant note: DOI: 10.13039/100000968, name: American Heart Association, award: 09GRNT2010084; DOI: 10.13039/501100001809, name: National Natural Science Foundation of China, award: 30872790/H0908; DOI: 10.13039/501100002338, name: Ministry of Education of the People's Republic of China, award: [2007 3020; DOI: 10.13039/501100004543, name: China Scholarship Council; DOI: 10.13039/100000002, name: National Institutes of Health, award: R01 AI090901
Language: English
Date published: 2010
Academic Unit: Pathology
Record Identifier: 9984047732602771

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