Modulation of PI3K/PTEN Pathway Does Not Affect Catalytic Activity Of
ANTICANCER RESEARCH 37 : 5415-5423 (2017) doi:10.21873/anticanres.11969 Modulation of PI3K/PTEN Pathway Does Not Affect Catalytic Activity of PDK1 in Jurkat Cells KEUM-JIN YANG 1, LONGZHEN PIAO 1,2 , SANGHEE SHIN 1, SO-YEON SHIN 1, YUWEN LI 1,3 , HYUNJI LEE 1, QUANGDON TRAN 1, JISOO PARK 1, SUNTAEK HONG 4, DEREK P. BRAZIL 5, BRIAN A. HEMMINGS 6, SEON-HWAN KIM 7 and JONGSUN PARK 1 1Metabolic Syndrome and Cell Signaling Laboratory, Department of Pharmacology and Medical Science, Institute for Cancer Research, and 7Department of Neurosurgery, Institute for Cancer Research, College of Medicine, Chungnam National University, Daejeon, Republic of Korea; 2Department of Oncology, Yanbian University Hospital, Yanji, P.R. China; 3Department of Pharmacy, Xijing Hospital, Fourth Military Medical University, Xi’an, P.R. China; 4Laboratory of Cancer Cell Biology, Department of Biochemistry, School of Medicine, Gachon University, Incheon, Republic of Korea; 5Centre for Experimental Medicine, Queen's University Belfast, Belfast, Northern Ireland, U.K.; 6Friedrich Miescher Institute for Biomedical Research, Basel, Switzerland Abstract. Unopposed phosphoinositide 3-kinase (PI3K) We demonstrated that reducing the level of 3- activity and 3-phosphoinositide production in Jurkat cells, phosphoinositides in Jurkat cells with pharmacological due to a mutation in the phosphatase and tensin homolog inhibitors of PI3K or expression of PTEN does not affect deleted on chromosome 10 (PTEN) tumor-suppressor PDK1 activity or its intracellular localization. We conclude, protein, results in deregulation of PH domain-containing therefore, that although Jurkat cells lack PTEN expression, proteins including the serine/threonine kinase PKB. In Jurkat only a subset of pathways downstream of PDK1 are cells, PKB is constitutively active and phosphorylated at the perturbed as a consequence of PTEN loss.
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