PDK1, the master regulator of AGC kinase signal transduction. Export

@article{citeulike:466957, abstract = {The interaction of insulin and growth factors with their receptors on the outside surface of a cell, leads to the activation of phosphatidylinositol 3-kinase (PI 3-kinase) and generation of the phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3) second messenger at the inner surface of the cell membrane. One of the most studied signalling events controlled by PtdIns(3,4,5)P3, comprises the activation of a group of AGC family protein kinases, including isoforms of protein kinase B (PKB)/Akt, p70 ribosomal S6 kinase (S6K), serum- and glucocorticoid-induced protein kinase (SGK) and protein kinase C (PKC), which play crucial roles in regulating physiological processes relevant to metabolism, growth, proliferation and survival. Here, we review recent biochemical, genetic and structural studies on the 3-phosphoinositide-dependent protein kinase-1 (PDK1), which phosphorylates and activates the AGC kinase members regulated by PI 3-kinase. We also discuss whether inhibitors of PDK1 might have chemotherapeutic potential in the treatment of cancers in which the PDK1-regulated AGC kinases are constitutively activated.}, address = {MRC Protein Phosphorylation Unit, MSI/WTB Complex, University of Dundee, Dow Street, Dundee DD1 5EH, Scotland, UK.}, author = {Mora, A. and Komander, D. and van Aalten, D. M. and Alessi, D. R.}, citeulike-article-id = {466957}, citeulike-linkout-0 = {http://view.ncbi.nlm.nih.gov/pubmed/15209375}, citeulike-linkout-1 = {http://www.hubmed.org/display.cgi?uids=15209375}, comment = {reactin 97}, issn = {1084-9521}, journal = {Semin Cell Dev Biol}, keywords = {pip3, tcrmr}, month = {April}, number = {2}, pages = {161--170}, posted-at = {2006-06-28 11:33:29}, priority = {5}, title = {PDK1, the master regulator of AGC kinase signal transduction.}, url = {http://view.ncbi.nlm.nih.gov/pubmed/15209375}, volume = {15}, year = {2004} }

TY - JOUR ID - citeulike:466957 L3 - citeulike-article-id:466957 N2 - The interaction of insulin and growth factors with their receptors on the outside surface of a cell, leads to the activation of phosphatidylinositol 3-kinase (PI 3-kinase) and generation of the phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3) second messenger at the inner surface of the cell membrane. One of the most studied signalling events controlled by PtdIns(3,4,5)P3, comprises the activation of a group of AGC family protein kinases, including isoforms of protein kinase B (PKB)/Akt, p70 ribosomal S6 kinase (S6K), serum- and glucocorticoid-induced protein kinase (SGK) and protein kinase C (PKC), which play crucial roles in regulating physiological processes relevant to metabolism, growth, proliferation and survival. Here, we review recent biochemical, genetic and structural studies on the 3-phosphoinositide-dependent protein kinase-1 (PDK1), which phosphorylates and activates the AGC kinase members regulated by PI 3-kinase. We also discuss whether inhibitors of PDK1 might have chemotherapeutic potential in the treatment of cancers in which the PDK1-regulated AGC kinases are constitutively activated. IS - 2 JF - Semin Cell Dev Biol SN - 1084-9521 AD - MRC Protein Phosphorylation Unit, MSI/WTB Complex, University of Dundee, Dow Street, Dundee DD1 5EH, Scotland, UK. EP - 170 TI - PDK1, the master regulator of AGC kinase signal transduction. VL - 15 SP - 161 KW - pip3 KW - tcrmr N1 - reactin 97 AU - Mora, A AU - Komander, D AU - van Aalten, DM AU - Alessi, DR PY - 2004/04// UR - http://view.ncbi.nlm.nih.gov/pubmed/15209375 ER -