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RETRACTED ARTICLE

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Anticancer Res. 2017 Oct;37(10):5415-5423.

Modulation of PI3K/PTEN Pathway Does Not Affect Catalytic Activity of PDK1 in Jurkat Cells.

Author information

1
Metabolic Syndrome and Cell Signaling Laboratory, Department of Pharmacology and Medical Science, Institute for Cancer Research, College of Medicine, Chungnam National University, Daejeon, Republic of Korea.
2
Department of Oncology, Yanbian University Hospital, Yanji, P.R. China.
3
Department of Pharmacy, Xijing Hospital, Fourth Military Medical University, Xi'an, P.R. China.
4
Laboratory of Cancer Cell Biology, Department of Biochemistry, School of Medicine, Gachon University, Incheon, Republic of Korea.
5
Centre for Experimental Medicine, Queen's University Belfast, Belfast, Northern Ireland, U.K.
6
Friedrich Miescher Institute for Biomedical Research, Basel, Switzerland.
7
Department of Neurosurgery, Institute for Cancer Research, College of Medicine, Chungnam National University, Daejeon, Republic of Korea neons@cnu.ac.kr insulin@cnu.ac.kr.
8
Metabolic Syndrome and Cell Signaling Laboratory, Department of Pharmacology and Medical Science, Institute for Cancer Research, College of Medicine, Chungnam National University, Daejeon, Republic of Korea neons@cnu.ac.kr insulin@cnu.ac.kr.

Retraction in

Abstract

Unopposed phosphoinositide 3-kinase (PI3K) activity and 3-phosphoinositide production in Jurkat cells, due to a mutation in the phosphatase and tensin homolog deleted on chromosome 10 (PTEN) tumor-suppressor protein, results in deregulation of PH domain-containing proteins including the serine/threonine kinase PKB. In Jurkat cells, PKB is constitutively active and phosphorylated at the activation-loop residue (Thr308). 3-Phosphoinositide-dependent protein kinase-1 (PDK1), an enzyme that also contains a PH domain, catalyses Thr308 phosphorylation of PKB in addition to other kinase families such as PKC isoforms. It is unknown, however, whether the loss of PTEN in Jurkat cells also results in unregulated PDK1 activity and whether such loss has an impact on activation-loop phosphorylation of other PDK1 substrates e.g. PKC. In this study, we addressed whether loss of PTEN in Jurkat cells affects PDK1 catalytic activity and intracellular localization. We demonstrated that reducing the level of 3-phosphoinositides in Jurkat cells with pharmacological inhibitors of PI3K or expression of PTEN does not affect PDK1 activity or its intracellular localization. We conclude, therefore, that although Jurkat cells lack PTEN expression, only a subset of pathways downstream of PDK1 are perturbed as a consequence of PTEN loss.

KEYWORDS:

Jurkat cells; PDK1; PI3K; PTEN; protein phosphorylation

PMID:
28982851
DOI:
10.21873/anticanres.11969
[Indexed for MEDLINE]

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