Phosphorylation of the transcription factor forkhead family member FKHR by protein kinase B
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TLDR
FKHR, a human homologue of the DAF16 transcription factor in Caenorhabditis elegans, is rapidly phosphorylated by human protein kinase Bα (PKBα) at Thr-24, Ser-256, and Ser-319 in vitro and at a much faster rate than BAD, which is thought to be a physiological substrate for PKB.About:
This article is published in Journal of Biological Chemistry.The article was published on 1999-06-11 and is currently open access. It has received 729 citations till now. The article focuses on the topics: Akt/PKB signaling pathway & Protein kinase B.read more
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Cellular survival: a play in three Akts
TL;DR: The mechanisms by which survival factors regulate the PI3K/c-Akt cascade, the evidence that activation of the PI 3K/ c-AKT pathway promotes cell survival, and the current spectrum of c- akt targets and their roles in mediating c- Akt-dependent cell survival are reviewed.
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The PI3K-PDK1 connection: more than just a road to PKB.
TL;DR: The mechanism by which PKB is activated and the downstream actions of this multifunctional kinase are reviewed, as well as the evidence that PDK1 may be involved in the activation of protein kinases other than PKB, and the possibility that some of the currently postulated PKB substrates targets might in fact be phosphorylated byPDK1-regulated kinasesother than P KB.
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Synthesis and Function of 3-Phosphorylated Inositol Lipids
Bart Vanhaesebroeck,Sally J. Leevers,Khatereh Ahmadi,John F. Timms,Roy Katso,Paul C. Driscoll,Rudiger Woscholski,Peter J. Parker,Michael D. Waterfield +8 more
TL;DR: This review is focused on the 3-phosphoinositide lipids, the synthesis of which is acutely triggered by extracellular stimuli, the enzymes responsible for their synthesis and metabolism, and their cell biological roles.
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The protein kinase B/Akt signalling pathway in human malignancy.
TL;DR: Recent developments in understanding the mechanisms and consequences of PKB/Akt activation in human malignancy are surveyed.
Journal ArticleDOI
The Ras-ERK and PI3K-mTOR pathways: cross-talk and compensation
TL;DR: The Ras-ERK and PI3K-mTOR signaling pathways were originally modeled as linear signaling conduits activated by different stimuli, yet even early experiments hinted that they might intersect to regulate each other and co-regulate downstream functions.
References
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Akt Promotes Cell Survival by Phosphorylating and Inhibiting a Forkhead Transcription Factor
Anne Brunet,Azad Bonni,Michael J. Zigmond,Michael Z. Lin,Peter Juo,Linda Hu,Michael J. Anderson,Karen C. Arden,John Blenis,Michael E. Greenberg +9 more
TL;DR: It is demonstrated that Akt also regulates the activity of FKHRL1, a member of the Forkhead family of transcription factors, which triggers apoptosis most likely by inducing the expression of genes that are critical for cell death, such as the Fas ligand gene.
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Akt Phosphorylation of BAD Couples Survival Signals to the Cell-Intrinsic Death Machinery
Sandeep Robert Datta,Henryk Dudek,Xu Tao,Shane C. Masters,Haian Fu,Yukiko Gotoh,Michael E. Greenberg +6 more
TL;DR: It is shown that growth factor activation of the PI3'K/Akt signaling pathway culminates in the phosphorylation of the BCL-2 family member BAD, thereby suppressing apoptosis and promoting cell survival.
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Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B.
TL;DR: It is shown that agents which prevent the activation of both MAPKAP kinase-1 and p70S6k by insulin in vivo do not block the phosphorylation and inhibition of GSK3, and it is demonstrated that PKB is the product of the proto-oncogene protein kinase B (PKB, also known as Akt/RAC).
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PD 098059 Is a Specific Inhibitor of the Activation of Mitogen-activated Protein Kinase Kinase in Vitro and in Vivo
TL;DR: The results indicate that the activation of Raf is suppressed and that its inactivation is accelerated by a downstream component(s) of the MAP kinase pathway.
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Characterization of a 3-phosphoinositide-dependent protein kinase which phosphorylates and activates protein kinase Bα
Dario R. Alessi,Stephen R. James,C. Peter Downes,Andrew B. Holmes,Piers R. J. Gaffney,Colin B. Reese,Philip Cohen +6 more
TL;DR: In this paper, a protein kinase that phosphorylates PKB α at Thr308 and increases its activity over 30-fold was found to play a key role in mediating the activation of PKB by insulin and growth factors.