ArticleJournal of chemical biology2009
3-D structure and dynamics of protein kinase B-new mechanism for the allosteric regulation of an AGC kinase.
Article in Journal of chemical biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed.
- Structural and mechanistic basis of mTORC2 activation of protein kinase AKT/PKB.The Biochemical journal · 2026Review
- Novel Allosteric Inhibitor-Derived AKT Proteolysis Targeting Chimeras (PROTACs) Enable Potent and Selective AKT Degradation in KRAS/BRAF Mutant Cells.Journal of medicinal chemistry · 2022Article
- Structure of autoinhibited Akt1 reveals mechanism of PIPProceedings of the National Academy of Sciences of the United States of America · 2021Article
- Inositol Polyphosphate-Based Compounds as Inhibitors of Phosphoinositide 3-Kinase-Dependent Signaling.International journal of molecular sciences · 2020Review
- Inhibitors in AKTion: ATP-competitive vs allosteric.Biochemical Society transactions · 2020Review
- Lipid-dependent Akt-ivity: where, when, and how.Biochemical Society transactions · 2019Review
- Getting the Akt Together: Guiding Intracellular Akt Activity by PI3K.Biomolecules · 2019Review
- Polyphosphoinositide-Binding Domains: Insights from Peripheral Membrane and Lipid-Transfer Proteins.Advances in experimental medicine and biology · 2019Review
- Akt-ing Up Just About Everywhere: Compartment-Specific Akt Activation and Function in Receptor Tyrosine Kinase Signaling.Frontiers in cell and developmental biology · 2019Review
- Conformational sampling of membranes by Akt controls its activation and inactivation.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Article
- Differential crosstalk between the AMPK and PI3K/Akt pathways in breast cancer cells of differing genotypes: Leptin inhibits the effectiveness of AMPK activation.Oncology reports · 2015Article
- SUMOylation regulates AKT1 activity.Oncogene · 2015Article
- Dual fluorescent molecular substrates selectively report the activation, sustainability and reversibility of cellular PKB/Akt activity.Scientific reports · 2013Article
- The Paradox of Akt-mTOR Interactions.Frontiers in oncology · 2013Article
- Disruption of PH-kinase domain interactions leads to oncogenic activation of AKT in human cancers.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Clinical proteomics and OMICS clues useful in translational medicine research.Proteome science · 2012Article
- Assembly of membrane-bound protein complexes: detection and analysis by single molecule diffusion.Biochemistry · 2012Article
- Effects of ethanol on conformational changes of Akt studied by chemical cross-linking, mass spectrometry, and (18)O labeling.ACS chemical biology · 2012Article
- Autoregulation of kinase dephosphorylation by ATP binding in AGC protein kinases.Cell cycle (Georgetown, Tex.) · 2012Review
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
New developments regarding the structure and in vivo dynamics of protein kinase B (PKB/Akt) have been recently exposed. Here, we specifically review how the use of multi-disciplinary approaches has resulted in reaching the recent progress made to relate the quaternary structure of PKB to its in vivo function. Using X-ray crystallography, the structure of PKB pleckstrin homology (PH) and kinase domains was determined separately. The molecular mechanisms involved in (a) the binding of the phosphoinositides to the PH domain and (b) the activation of the kinase with the rearrangement of the catalytic site and substrate binding were determined. In vitro, nuclear magnetic resonance and circular dychroism studies gave complementary information on the interaction of the PH domain with the phosphoinositides. However, the molecular nature and the function of the interactions between the PKB domains could not be deduced from the X-ray data since the full-length PKB has not been crystallised. In vitro, dynamic information on the inter-domain conformational changes related to PKB activation states emerged with the use of tandem mass spectrometry. Cell imaging and Förster resonance energy transfer provided in vivo dynamics. Molecular modelling and dynamic simulations in conjunction with mutagenesis and biochemical analysis were used to investigate the complex interactions between the PKB domains in vivo and understand at the molecular level how it linked to its activity. The compilation of the information obtained on the 3-D structure and the spatiotemporal dynamics of this widely studied oncogene could be applied to the study of other proteins. This inter-disciplinary approach led to a more profound understanding of PKB complex activation mechanism in vivo that will shed light onto new ideas and possibilities for modulating its activity.
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Registered trials
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