Protein kinase B kinases that mediate phosphatidylinositol 3,4,5-trisphosphate-dependent activation of protein kinase B.

@article{Stephens1998ProteinKB,
  title={Protein kinase B kinases that mediate phosphatidylinositol 3,4,5-trisphosphate-dependent activation of protein kinase B.},
  author={Len R. Stephens and Karen E. Anderson and David Stokoe and Hediye Erdjument-Bromage and Gavin F. Painter and Andrew B. Holmes and Piers R. J. Gaffney and Colin B. Reese and Frank McCormick and Paul Tempst and John Coadwell and Phillip T. Hawkins},
  journal={Science},
  year={1998},
  volume={279 5351},
  pages={
          710-4
        }
}
Protein kinase B (PKB) is activated in response to phosphoinositide 3-kinases and their lipid products phosphatidylinositol 3,4, 5-trisphosphate [PtdIns(3,4,5)P3] and PtdIns(3,4)P2 in the signaling pathways used by a wide variety of growth factors, antigens, and inflammatory stimuli. PKB is a direct target of these lipids, but this regulation is complex. The lipids can bind to the pleckstrin homologous domain of PKB, causing its translocation to the membrane, and also enable upstream, Thr308… Expand
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References

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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
Protein kinase B (c-Akt) in phosphatidylinositol-3-OH kinase signal transduction
TLDR
A role for PKB in PI(3)K-mediated signal transduction is suggested and a constructed Gag–PKB fusion protein, homologous to the v-akt oncogene, displays significantly increased ligand-independent kinase activity. Expand
Dual role of phosphatidylinositol-3,4,5-trisphosphate in the activation of protein kinase B.
TLDR
Chromatographic separation of brain cytosol revealed a kinase activity that phosphorylated and activated PKB only in the presence of phosphatidylinositol-3, 4,5-trisphosphate [PtdIns(3,4,5)P3]. Expand
Membrane localization of phosphatidylinositol 3-kinase is sufficient to activate multiple signal-transducing kinase pathways
TLDR
The results show that PI 3-kinase activation is sufficient to stimulate several kinases that appear to function in different signaling pathways, including the stimulation of pp70 S6 kinase, Akt/Rac, and Jun N-terminal kinase (JNK). Expand
Specific binding of the Akt-1 protein kinase to phosphatidylinositol 3,4,5-trisphosphate without subsequent activation.
Recent evidence has suggested that activation of phosphoinositide 3-kinase (PI 3-kinase) is required for the activation of Akt-1 by growth factors and insulin. Here we demonstrate by two independentExpand
The protein kinase encoded by the Akt proto-oncogene is a target of the PDGF-activated phosphatidylinositol 3-kinase
TLDR
It is shown that Akt and the Akt-related kinase AKT2 are activated by PDGF, and it is suggested that the AkT PH domain may be a mediator of PI 3-kinase signaling. Expand
Activation of the zeta isozyme of protein kinase C by phosphatidylinositol 3,4,5-trisphosphate.
TLDR
The results suggest that PKC zeta may be a target for PIP3 and thus may be involved in the signaling mechanism(s) for growth factors and oncogenes that increase phosphatidylinositol 3-kinase activity. Expand
Akt, a Pleckstrin Homology Domain Containing Kinase, Is Activated Primarily by Phosphorylation*
TLDR
It is shown, in three cell types, that Akt does not require its pleckstrin homology domain to respond to either insulin or platelet-derived growth factor, and the primary mechanism of Akt activation is via protein phosphorylation. Expand
Activation of protein kinase C family members by the novel polyphosphoinositides PtdIns-3,4-P2 and PtdIns-3,4,5-P3.
TLDR
These lipids could act as second messengers to activate PKC delta, epsilon, or eta in vivo and are nominally absent in unstimulated cells and appear within seconds to minutes of stimulation by various cell activators. Expand
PDGF stimulates an increase in GTP–Rac via activation of phosphoinositide 3-kinase
TLDR
It is shown that platelet-derived growth factor can stimulate an increase in the level of GTP-Rac by at least two distinct mechanisms: firstly, by increased guanine nucleotide exchange; and secondly, by inhibition of a Rac GTPase activity. Expand
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