EC Number   |
General Information |
Reference |
|---|
   3.1.3.67 | malfunction |
deletion of SidF results in the reduced recruitment of effector proteins that anchor on the Legionella-containing vacuole (LCV) via binding to PI(4)P |
732810 |
| 3.1.3.67 | malfunction |
in PTEN siRNA transfected cells, insulin treatment showed a remarkable increase in PIP3 compared with control cells. PI(3,4)P2 levels are not altered in siRNA-transfected cells. PTEN-knockdown results in an increase in PIP3 levels under basal conditions compared to control cells.Silencing of SKIP, increases the insulin-dependent recruitment of GLUT4 vesicles to the plasma membrane |
732083 |
| 3.1.3.67 | malfunction |
lentiviral infection of PTEN shRNA significantly inhibits Caco-2/15 cell polarization, functional differentiation and brush border development. A strong reduction in claudin 1, 3, 4 and 8 is also observed as well as a decrease in transepithelial resistance. Loss of PTEN phosphatase expression increases the spreading, migration and invasion capacities of colorectal cancer cells in vitro, role of PTEN in human colorectal cancer cells, phenotype, overview. Loss of PTEN expression in Caco-2/15 cells stimulates migration/invasion, promotes tumor growth but is not sufficient to confer metastatic potential in vivo |
716688 |
| 3.1.3.67 | malfunction |
thrombin transiently increases PTEN lipid phosphatase activity, while pretreatment of HPAE cells with bpV(pic) slightly reduces basal PTEN activity.Thrombin fails to induce PTEN activity in cells pretreated with bpV(pic). Inhibiting PTEN activity also decreases Akt phosphorylation, inhibiting PTEN phosphatase activity has no effect on thrombin-induced Ca2+ entry |
715544 |
| 3.1.3.67 | more |
loss of PTEN expression in HCT116 and CT26, but not in Caco-2/15, leads to an increase in their metastatic potential following tail-vein injections in mice |
716688 |
| 3.1.3.67 | physiological function |
phosphatase and tensin homologue is a dual lipidprotein phosphatase that catalyzes the conversion of phosphoinositol 3,4,5-triphosphate to phosphoinositol 4,5-bisphosphate and thereby inhibits PI3K-Akt-dependent cell proliferation, migration, and tumor vascularization. But PTEN is indicated to play a role beyond suppressing PI3K signaling, it also plays a role in regulating Ca2+ entry through transient receptor potential canonical channel 6, TRPC6, that does not require PTEN phosphatase activity, overview. PTEN tail-domain residues 394-403 permit PTEN to associate with TRPC6. The inflammatory mediator thrombin promotes this association. Deletion of PTEN residues 394-403 prevents TRPC6 cell surface expression and Ca2+ entry, regulation, overview |
715544 |
| 3.1.3.67 | physiological function |
the baseline level of phosphatidylinositol-3,4,5-triphosphate influences cell susceptibility to the toxic effects of Aggregatibacter actinomycetemcomitans cytolethal distending toxin Cdt. Jurkat cells with known defects in phosphatidylinositol-3,4,5-triphosphate degradative enzymes, PTEN and SHIP1, contain high baseline levels of PIP3, pAkt, and pGSK3b, and also exhibit high sensitivity to Cdt-HUT78 cells, with no known defects in this pathway, contain low levels of PIP3, pAkt, and pGSK3b and exhibit reduced susceptibility to Cdt. Jurkat and HUT78 cells bind toxin at comparable levels and internalize relatively equal amounts of active subunit CdtB |
751604 |
