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Characterization of a 3-phosphoinositide-dependent protein kinase which phosphorylates and activates protein kinase Bα
BACKGROUND Protein kinase B (PKB), also known as c-Akt, is activated rapidly when mammalian cells are stimulated with insulin and growth factors, and much of the current interest in this enzyme stemsExpand
The TSC1-2 tumor suppressor controls insulin–PI3K signaling via regulation of IRS proteins
The results argue that the low malignant potential of tumors arising from TSC1-2 dysfunction may be explained by the failure of TSC mutant cells to activate PI3K and its downstream effectors. Expand
The lipid phosphatase activity of PTEN is critical for its tumor supressor function.
  • M. Myers, I. Pass, +6 authors N. Tonks
  • Biology, Medicine
  • Proceedings of the National Academy of Sciences…
  • 10 November 1998
It is reported that a missense mutation in PTEN, PTEN-G129E, which is observed in two Cowden disease kindreds, specifically ablates the ability of PTEN to recognize inositol phospholipids as a substrate, suggesting that loss of the lipid phosphatase activity is responsible for the etiology of the disease. Expand
Identification of pleckstrin-homology-domain-containing proteins with novel phosphoinositide-binding specificities.
This study lays the foundation for future work to establish the phospholipid-binding specificities of these proteins in vivo, and their physiological role(s). Expand
Neural and developmental actions of lithium: A unifying hypothesis
Lithium, with an atomic weight of 6.9, is the smallest of the alkali metals, yet this simple ion can exert a profound effect on both human behavior and early embryonic devel- opment. Expand
Changes in the levels of inositol phosphates after agonist-dependent hydrolysis of membrane phosphoinositides.
The results suggest that the earliest event in the stimulus-response pathway is the hydrolysis of polyphosphoinositides by a phosphodiesterase to yield inositol 1,4,5-trisphosphate and inositl 1, 4-bisph phosphate, which are subsequently hydrolysed to inositoli 1-phosphates and inposol. Expand
Type I phosphatidylinositol kinase makes a novel inositol phospholipid, phosphatidylinositol-3-phosphate
It is proposed that type I Ptdlns kinase is responsible for the generation of PtdIns(3)P in intact cells, and that this novel phosphoinositide could be important in the transduction of mitogenic and oncogenic signals. Expand
PDK1 acquires PDK2 activity in the presence of a synthetic peptide derived from the carboxyl terminus of PRK2
PDK1 and PDK2 might be the same enzyme, the substrate specificity and activity of PDK1 being regulated through its interaction with another protein(s), and PRK2 is a probable substrate for PDK 1. Expand
Role of phosphatidylinositol 3,4,5-trisphosphate in regulating the activity and localization of 3-phosphoinositide-dependent protein kinase-1.
Results indicate that PtdIns(3,4,5)P3 plays several roles in the PDK1-induced activation of P KBalpha, and binds to the PH domain of PKB, altering its conformation so that it can be activated by PDK 1. Expand
Lithium amplifies agonist-dependent phosphatidylinositol responses in brain and salivary glands.
The ability of Li+ to greatly amplify the agonist-dependent accumulation of myo-inositol 1-phosphate offers a novel technique for identifying those receptors that function by hydrolysing phosphatidyl inositol, which may help reset the sensitivity of those multifunctional receptors that generate second messengers such as Ca2+, cyclic GMP and the prostaglandins. Expand