Phosphoinositide-Dependent Kinase-1 (PDK1) is an essential master kinase recruited to the plasma membrane by the binding of its C-terminal PH domain to the signaling lipid phosphatidylinositol-3,4-5-trisphosphate (PIP 3).

Jul 16, 2013 · Phosphoinositide-dependent kinase-1 (PDK1) is an essential master kinase recruited to the plasma membrane by the binding of its C-terminal PH domain to the signaling lipid phosphatidylinositol-3,4,5-trisphosphate (PIP3).

Apr 6, 2022 · We show that PDK1 trans -autophosphorylation is mediated by a PIP 3 -mediated face-to-face dimer. We report regulatory motifs in the kinase-PH interdomain linker that allosterically activate...

PDK1 interacts with phosphoinositides through a pleckstrin homology (PH) domain. To study the role of this interaction, we generated knock-in mice expressing a mutant of PDK1 incapable of binding phosphoinositides. The knock-in mice are significantly small, insulin resistant, and hyperinsulinemic.

Apr 6, 2022 · We show that PDK1 trans-autophosphorylation is mediated by a PIP 3-mediated face-to-face dimer. We report regulatory motifs in the kinase-PH interdomain linker that allosterically activate PDK1 autophosphorylation via a linker-swapped dimer mechanism.

Jul 29, 2013 · Our study suggests that the efficiency of therapies targeting the aberrantly activated PI3K/PDK1/Akt pathway might be increased by the parallel blockade of feedback circuits. The...

Oct 1, 1997 · We recently identified a protein kinase, termed PDK1, that phosphorylates PKB at Thr308 only in the presence of lipid vesicles containing phosphatidylinositol 3,4,5-trisphosphate (PtdIns (3,4,5)P 3) or phosphatidylinositol 3,4-bisphosphate (PtdIns (3,4)P 2). Results: We have cloned and sequenced human PDK1.

Phosphoinositide-dependent protein kinase-1 (PDK1) is a serine/threonine kinase. Structurally, PDK1 is constituted of two domains such as kinase domain also called the catalytic domain and the carboxyl-terminal pleckstrin homology domain.

Here, we report in vitro kinetic, phosphopeptide mapping, and oligomerization studies that address the role of the PH domain in regulating specific autophosphorylation events, which are required for PDK1 catalytic activation.

PDPK1 is a master kinase, which is crucial for the activation of AKT /PKB and many other AGC kinases including PKC, S6K, SGK. An important role for PDPK1 is in the signaling pathways activated by several growth factors and hormones including insulin signaling.