Regulation of the ABC kinases by phosphorylation: protein kinase C as a paradigm.
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TLDR
This review focuses on how phosphorylation at each of these sites regulates the maturation, signalling and down-regulation of PKC as a paradigm for how these sites control the function of the ABC kinases.Abstract:
Phosphorylation plays a central role in regulating the activation and signalling lifetime of protein kinases A, B (also known as Akt) and C. These kinases share three conserved phosphorylation motifs: the activation loop segment, the turn motif and the hydrophobic motif. This review focuses on how phosphorylation at each of these sites regulates the maturation, signalling and down-regulation of PKC as a paradigm for how these sites control the function of the ABC kinases.read more
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References
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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.
Mechanism of activation of protein kinase B by insulin and IGF-1. EMBO J 15 (23):6541-6551
TL;DR: It is demonstrated that activation of PKBalpha by insulin or insulin‐like growth factor‐1 (IGF‐1) results from phosphorylation of both Thr308 and Ser473, that phosphorylate of both residues is critical to generate a high level of P KBalpha activity and that the phosphorylated of Thr308 in vivo is not dependent on phosphorylations of Ser473 or vice versa.
Journal ArticleDOI
Mechanism of activation of protein kinase B by insulin and IGF-1.
Dario R. Alessi,Mirjana Andjelkovic,Barry Caudwell,Peter Cron,Nick Morrice,Philip Cohen,Brian A. Hemmings +6 more
TL;DR: In this paper, the activation of PKBalpha was accompanied by its phosphorylation at Thr308 and Ser473 and, like activation, likeactivation was prevented by the phosphatidylinositol 3-kinase inhibitor wortmannin.
Journal ArticleDOI
Protein kinase C and lipid signaling for sustained cellular responses.
TL;DR: It is now becoming evident that stimulation of a cell surface receptor initiates a degradation cascade of various membrane lipid constituents that has potentials to induce, intensify, and prolong the activation of protein kinase C that is needed for sustained cellular responses.
Journal ArticleDOI
Crystal Structure of the Catalytic Subunit of Cyclic Adenosine Monophosphate-Dependent Protein Kinase
Daniel R. Knighton,Jianhua Zheng,L. F. Ten Eyck,L. F. Ten Eyck,Victor A. Ashford,Nguyen-Huu Xuong,Susan S. Taylor,Janusz M. Sowadski +7 more
TL;DR: The crystal structure of the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase complexed with a 20-amino acid substrate analog inhibitor has been solved and partially refined at 2.7 A resolution to an R factor of 0.212.