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Papers In Press, published online ahead of print September 9, 2004
Division of Cell Biology, La Jolla Institute for Allergy and Immunology, San Diego, California 92121
Corresponding Author: toshi{at}liai.org
Akt (= protein kinase B), a subfamily of the AGC serine/threonine kinases, plays critical roles in survival, proliferation, glucose metabolism, and other cellular functions. Akt activation requires the recruitment of the enzyme to the plasma membrane by interacting with membrane-bound lipid products of phosphatidylinositol 3-kinase. Membrane-bound Akt is then phosphorylated at two sites for its full activation: Thr-308 in the activation loop of the kinase domain is phosphorylated by 3-phosphoinositide-dependent kinase-1 (PDK1) and Ser-473 in the C-terminal hydrophobic motif by a putative kinase PDK2. The identity of PDK2 has been elusive. Here we present evidence that conventional isoforms of protein kinase C (PKC), particularly PKC
J. Biol. Chem, 10.1074/jbc.M408797200
Submitted on August 2, 2004
Revised on September 8, 2004
Accepted on September 9, 2004
Protein kinase C
II regulates Akt phosphorylation on Ser-473 in a cell type- and stimulus-specific fashion
II, can regulate Akt activity by directly phosphorylating Ser-473 in vitro and in IgE/antigen-stimulated mast cells. By contrast, PKC is not required for Ser-473 phosphorylation in mast cells stimulated with stem cell factor or IL-3, in serum-stimulated fibroblasts, or in antigen receptor-stimulated T or B lymphocytes. Therefore, PKCII appears to work as a cell type- and stimulus-specific PDK2.
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