PKB/AKT: functional insights from genetic models View Full Text


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Article Info

DATE

2001-10

AUTHORS

Michael P. Scheid, James R. Woodgett

ABSTRACT

Key Points Since its discovery 10 years ago, studies have shown that PKB, also known as AKT, is an important enzyme in mediating the pro-survival signals of PI3K. Activation of PKB/AKT is complex and tightly controlled by the activities of upstream protein kinases such as PDK1, which targets the T-loop in the protein. A hypothesized kinase, called PDK2, has also been implicated in PKB/AKT activation. Candidates for this kinase include MAPK-activated protein kinase 2 (MAPKAP-K2), Rsk (MAPKAP-K1) and integrin-linked kinase (ILK). Identifying PKB/AKT substrates has been fundamental to understanding how the kinase impacts on insulin signalling, cell growth and apoptosis. PKB/AKT has been found to interact with factors, including the Forkhead family of transcription factors and GSK3, which indicates PKB/AKT might have several inputs into the control of the cell cycle. PKB/AKT activation cooperates with other genes in promoting cancer and inflammation. PTEN is a tumour suppressor that acts to inactivate PKB/AKT, as well as other PI3K-activated targets. Small molecule drugs that inhibit PKB/AKT may have therapeutic potential in cancer treatment. A relative of PKB/AKT, termed SGK/CISK, might cooperate with PKB in overlapping or distinct physiological functions. The difficulty will be to resolve the true functions of PKB/AKT and those of SGK/CISK, as it could be that SGK/CISK is responsible for some of the functions originally attributed to PKB/AKT. More... »

PAGES

760-768

References to SciGraph publications

  • 1999-09. NF-κB is a target of AKT in anti-apoptotic PDGF signalling in NATURE
  • 1995-12. Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B in NATURE
  • 2001-05-24. Phox domain interaction with PtdIns(3)P targets the Vam7 t-SNARE to vacuole membranes in NATURE CELL BIOLOGY
  • 1997-05. Germline mutations of the PTEN gene in Cowden disease, an inherited breast and thyroid cancer syndrome in NATURE GENETICS
  • 1999-06. Activation of nitric oxide synthase in endothelial cells by Akt-dependent phosphorylation in NATURE
  • 1999-12-23. Integrin-linked kinase regulates phosphorylation of serine 473 of protein kinase B by an indirect mechanism in ONCOGENE
  • 1999-11-10. Cell-autonomous regulation of cell and organ growth in Drosophila by Akt/PKB in NATURE CELL BIOLOGY
  • 2001-04. A motif-based profile scanning approach for genome-wide prediction of signaling pathways in NATURE BIOTECHNOLOGY
  • 1999-06. Regulation of endothelium-derived nitric oxide production by the protein kinase Akt in NATURE
  • 2001-06-12. PtdIns(3)P regulates the neutrophil oxidase complex by binding to the PX domain of p40phox in NATURE CELL BIOLOGY
  • 2000-04. AFX-like Forkhead transcription factors mediate cell-cycle regulation by Ras and PKB through p27kip1 in NATURE
  • 2001-06-12. The PX domains of p47phox and p40phox bind to lipid products of PI(3)K in NATURE CELL BIOLOGY
  • 2000-08-17. The conserved PI3′K/PTEN/Akt signaling pathway regulates both cell size and survival in Drosophila in ONCOGENE
  • 1994-08. Phosphatidylinositol-3-OH kinase direct target of Ras in NATURE
  • 1999-09. NF-κB activation by tumour necrosis factor requires the Akt serine–threonine kinase in NATURE
  • 1999-01. PIK3CA is implicated as an oncogene in ovarian cancer in NATURE GENETICS
  • 1999-04. Direct control of the Forkhead transcription factor AFX by protein kinase B in NATURE
  • 2000-05. Combined activation of Ras and Akt in neural progenitors induces glioblastoma formation in mice in NATURE GENETICS
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    URI

    http://scigraph.springernature.com/pub.10.1038/35096067

    DOI

    http://dx.doi.org/10.1038/35096067

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1047571972

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/11584303


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