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Regulation of the ABC kinases by phosphorylation: protein kinase C as a paradigm.

Alexandra C. Newton
- 01 Mar 2003 - 
- Vol. 370, Iss: 2, pp 361-371
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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.

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References
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Journal ArticleDOI

Characterization of a 3-phosphoinositide-dependent protein kinase which phosphorylates and activates protein kinase Bα

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.

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

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.
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