3.1.3.67 380-385A in endothelial cells transfected with 380-385A (mutation on the PTEN phosphorylation site) phosphatidylinositol 3,4,5-trisphosphate immunofluorescence intensity is than in wildtype or G129R transfected cells. Phosphatidylinositol 3,4,5-trisphosphate intensity in endothelial cells transfected with 380–385A is weak but gradually increases to a maximum at 240 min after cyclic strain stimulation by 1.48fold relative to static condition 681020 3.1.3.67 A121P inactive mutant enzyme 650767 3.1.3.67 C105F inactive mutant enzyme 650767 3.1.3.67 C124R inactive mutant enzyme 650767 3.1.3.67 C124S adenovirus encoding a dominant negative human PTEN cDNA is used for the transduction of cell cultures 692556 3.1.3.67 C124S catalytically inactive mutant enzyme 650763 3.1.3.67 C124S catalytically inert mutant enzyme 653626 3.1.3.67 C124S complete loss of activity towards inositol 1,3,4,5-tetrakisphosphate 651881 3.1.3.67 C124S mutant PTEN-C124S-A4-YFP lacks lipid and protein phosphatase activity, great localization to the plasma membrane than other mutants 694916 3.1.3.67 C124S phosphatase-deficient 705669 3.1.3.67 C124S PTEN mutant is devoid of phosphatase activity and fails to modulate p75NTR expression, indicating that phosphatase activity is required for PTEN regulation of neurotophin receptor p75NTR 690780 3.1.3.67 C124S the PTEN mutant lacks phosphatase activity, but is not altered in TRPC6 activity 715544 3.1.3.67 C136Y inactive mutant enzyme 650767 3.1.3.67 C645S inactive mutant 732810 3.1.3.67 C71Y inactive mutant enzyme 650767 3.1.3.67 D107Y inactive mutant enzyme 650767 3.1.3.67 D331G mutant enzyme with partial activity 650767 3.1.3.67 D92A catalytically inert mutant enzyme, retains partial ability to induce cells to accumulate in G1 653626 3.1.3.67 DELTA1-15 phosphatidylinositol 4,5-biphosphate has no effect on binding of PTEN16-403 690927 3.1.3.67 DELTA352-403 truncated enzyme binds strongly to the plasma membrane, an effect that is reversed by co-expression of the remainder of the molecule, PTEN 352-403 694916 3.1.3.67 DELTA394-403 removal of the last 10 residues of PTEN leads to the complete diffusion of PTEN in MDCK cells, failing to restore the junctional localization of phosphatidylinositol 4,5-bisphosphate 693117 3.1.3.67 F342N mutant enzyme with partial activity 650767 3.1.3.67 F347L mutant enzyme with partial activity 650767 3.1.3.67 G129E inactive mutant enzyme 650767 3.1.3.67 G129E mutant enzyme associated with Cowden‘s disease has protein phosphatase activity yet is defective in dephosphorylating inositol 1,3,4,5-tetrakisphosphate in vitro and fails to arrest cells in G1 653626 3.1.3.67 G129E mutant enzyme is selectively deficient in the lipid phosphatase activity but still blocks the cell cycle of MCF-7 cells 651205 3.1.3.67 G129E phosphatase-deficient 705669 3.1.3.67 G129E protein phosphatase-active, lipid phosphatase inactive mutant, expression of G129E mutant of PTEN in U-87MG cells has no effect on the phosphorylation status of protein kinase B, the mutant displays 7% of wildtype lipid phosphatidylinositol 3,4,5-trisphosphate-phosphatase activitiy and 65% wild type protein phosphatase activitiy in glioma cells 691607 3.1.3.67 G129E PTEN mutant which is lipid phosphatase dead but which retains protein phosphatase activity, significantly reduces the expression of p75NTR, suggesting that it is the protein phosphatase activity of PTEN that is able to regulate neurotophin receptor p75NTR expression 690780 3.1.3.67 G129E transduction of recombinant PTEN in to TMK-1 cells promotes nuclear localization with increased mRNA levels of CDX2 and intestinal claudins, whereas the G129 dead phosphatase mutant has no effect 691598 3.1.3.67 G129R in endothelial cells transfected with G129R, that lacks both protein and lipid phosphatase activities, phosphatidylinositol 3,4,5-trisphosphate immunofluorescence intensity is higher than transfection with wildtype PTEN. phosphatidylinositol 3,4,5-trisphosphate immunofluorescence in endothelial cells transfected with G129R rapidly increases and is maximum at 60 min after cyclic strain stimulation by 2.14fold relative to static condition 681020 3.1.3.67 G129R inactive mutant enzyme 650767 3.1.3.67 G129R the enzyme fails to induce a G1 block 653626 3.1.3.67 G165R inactive mutant enzyme 650767 3.1.3.67 G20E mutant enzyme with partial activity 650767 3.1.3.67 G251C inactive mutant enzyme 650767 3.1.3.67 H123Y mutant enzyme lacking phosphatase activity is ineffective in blocking the cell cycle of MCF-7 cells 651205 3.1.3.67 H129R mutant enzyme lacking phosphatase activity is ineffective in blocking the cell cycle of MCF-7 cells 651205 3.1.3.67 H61R inactive mutant enzyme 650767 3.1.3.67 H93Y inactive mutant enzyme 650767 3.1.3.67 K13E the binding of the PTEN mutant K13E, which is a tumor-derived mutation that renders PTEN inactive, is not affected by phosphatidylinositol 4,5-biphosphate 690927 3.1.3.67 K289E mutant enzyme with partial activity 650767 3.1.3.67 L112P inactive mutant enzyme 650767 3.1.3.67 L112R inactive mutant enzyme 650767 3.1.3.67 L345Q inactive mutant enzyme 650767 3.1.3.67 L42R activity is comparable with or even higher than that of wild-type enzyme 650767 3.1.3.67 M134L mutant enzyme with partial activity 650767 3.1.3.67 additional information adipose tissue-specific depletion of PTEN in mice results in improved glucose tolerance and insulin sensitivity rendering mice resistant to streptozotocin-induced diabetes. Increased recruitment of Glut4 transporters at the plasma membrane of adipocytes,whereas the contrary is observed in muscle of the same animals. Decreased expression of resistin is shown 677869 3.1.3.67 additional information CA1 synapses in hippocampal slices from PTEN-deficient mice exhibit activity-induced long-term potentiation of synaptic transmission but are resistant to long-term depression. PTEN reduces phosphatidylinositol-3-kinase activity and pharmacological inhibition of phosphatidylinositol-3-kinase restores long-term depression of synaptic transmission in PTEN-deficient mice, suggesting that inhibition of phosphatidylinositol-3-kinase is necessary for induction of long term depression 682123 3.1.3.67 additional information deletion of one PTEN allele in insulin receptor substrate 2 (IRS2) in mice is able to restore pancreatic beta-cell function, peripheral insulin sensitivity, glucose tolerance and significantly increases life span of the animals, indicating that PTEN controls insulin sensitivity in peripheral tissues and pancreatic beta-cell growth and function 677869 3.1.3.67 additional information deletion of the C-terminal portion of SidF including the two transmembrane motifs changes its localization to the cell periphery 732810 3.1.3.67 additional information deletion of the putative transmembrane domains does not affect its enzymatic activity 732810 3.1.3.67 additional information lentiviral infection of PTEN shRNA significantly inhibited Caco-2/15 cell polarization, functional differentiation and brush border development 716688 3.1.3.67 additional information liver-specific deletion of PTEN in mice results in enhanced insulin sensitivity, hypoinsulinemia, hypoleptinemia and overall improved glucose tolerance. Adult mice lacking PTEN in liver also develop hepatomegaly syndromes, steatohepatitis and hepatocellular carcinomas 677869 3.1.3.67 additional information muscle-specific depletion of PTEN in mice results in improved glucose metabolism in animals with diabetes and insulin resistance. Elevated fasting glucose levels are prevented and insulin sensitivity and glucose tolerance in high-fat fed animals are improved. Insulin stimulated Akt-activation is enhanced. PTEN depletion in muscle is not associated with increased tumorigenesis 677869 3.1.3.67 additional information overexpresion of catalytically inactive or dominant-negative PTEN mutants in 3T1-L1 adipocytes show that it is the lipid phosphatase activity of PTEN which is required to downregulate Akt/PKB signaling and glucose uptake in response to insulin 677869 3.1.3.67 additional information PTEN downregulation in 3T1-L1 adipocytes by small interfering RNAs enhances Akt/PKB activation and glucose uptake in response to insulin 677869 3.1.3.67 additional information PTEN null mutations in mice are lethal at embryonic stages and even a 50% reduction in PTEN expression leads to increased tumorigenesis 677869 3.1.3.67 additional information PTEN overexpression in 3T1-L1 adipocytes causes inhibition of insulin-induced PtdIns(3,4)P2 and PtdIns(3,4,5)P3 production, Akt/PKB activation, GLUT4 translocation to the cell membrane and glucose uptake 677869 3.1.3.67 additional information PTEN overexpression in MCF-7 breast cancer cell line prevents ERK1/2 phosphorylation in response to insulin. Inhibition of ERK1/2 activation is not only caused by a reduction in PtdIns(3,4,5)P3 level but also by a decreased association of Shc with Grb2/Sos complex and Ras activation 677869 3.1.3.67 PTEN1-274 when produced as glutathione S-transferase fusion protein, the protein is defective in catalyzing the release of phosphate from either a phosphate-labeled poly(Glu4-Tyr1) substrate or inositol 1,3,4,5-tetrakisphosphate 653626 3.1.3.67 PTEN1-336 when produced as glutathione S-transferase fusion protein, the protein is defective in catalyzing the release of phosphate from either a phosphate-labeled poly(Glu4-Tyr1) substrate or inositol 1,3,4,5-tetrakisphosphate 653626 3.1.3.67 PTENDELTA274-342 when produced as glutathione S-transferase fusion protein, the protein is defective in catalyzing the release of phosphate from either a phosphate-labeled poly(Glu4-Tyr1) substrate or inositol 1,3,4,5-tetrakisphosphate 653626 3.1.3.67 R130G inactive mutant enzyme 650767 3.1.3.67 R130L inactive mutant enzyme 650767 3.1.3.67 R130M kinase dead mutant, expression of R130M mutant of PTEN in U-87MG cells has no effect on the phosphorylation status of protein kinase B, the mutant displays 5% of wildtype lipid phosphatidylinositol 3,4,5-trisphosphate-phosphatase activitiy and 12% of wild-type protein phosphatase activitiy in glioma cells 691607 3.1.3.67 R130Q inactive mutant enzyme 650767 3.1.3.67 R173C inactive mutant enzyme 650767 3.1.3.67 R173H inactive mutant enzyme 650767 3.1.3.67 R173P inactive mutant enzyme 650767 3.1.3.67 S10N activity is comparable with or even higher than that of wild-type enzyme 650767 3.1.3.67 S170N inactive mutant enzyme 650767 3.1.3.67 S170R inactive mutant enzyme 650767 3.1.3.67 S227F mutant enzyme with partial activity 650767 3.1.3.67 S380A greater catalytic activity than an unphosphorylated, bacterially expressed wild type enzyme 694495 3.1.3.67 S380A PTEN-green fluorescent protein mutant shows significant localization to the plasma membrane, the effect requires no catalytic activity 694916 3.1.3.67 S383A PTEN-green fluorescent protein mutant shows significant localization to the plasma membrane, the effect requires no catalytic activity 694916 3.1.3.67 T382A greater catalytic activity than an unphosphorylated, bacterially expressed wild type enzyme 694495 3.1.3.67 T382A PTEN-green fluorescent protein mutant shows significant localization to the plasma membrane, the effect requires no catalytic activity 694916 3.1.3.67 T383A greater catalytic activity than an unphosphorylated, bacterially expressed wild type enzyme 694495 3.1.3.67 T385A PTEN-green fluorescent protein mutant shows significant localization to the plasma membrane, the effect requires no catalytic activity 694916 3.1.3.67 T401I activity is comparable with or even higher than that of wild-type enzyme 650767 3.1.3.67 V133I inactive mutant enzyme 650767 3.1.3.67 V343E inactive mutant enzyme 650767 3.1.3.67 V369G activity is comparable with or even higher than that of wild-type enzyme 650767 3.1.3.67 Y155C inactive mutant enzyme 650767 3.1.3.67 Y16C inactive mutant enzyme 650767 3.1.3.67 Y174N inactive mutant enzyme 650767 3.1.3.67 Y27S inactive mutant enzyme 650767 3.1.3.67 Y68H inactive mutant enzyme 650767