The Par6α/aPKC complex regulates Akt1 activity by phosphorylating Thr34 in the PH-domain

Molecular and Cellular Endocrinology

Volumn 268, Issue 1-2, 2007, Pages 30-36

  Weyrich, P ^a   Neuscheler, D ^a   Melzer, M ^a   Hennige, A M ^a   Haring H U ^a   Lammers, R ^a  

^a UNIVERSITY OF TÜBINGEN   (Germany)

Author keywords

Akt1; Atypical protein kinase C; Glycogen synthesis; Insulin resistance; Insulin signalling; Par6

Indexed keywords

INSULIN; PROTEIN; PROTEIN 6ALPHA; PROTEIN KINASE; PROTEIN KINASE C; UNCLASSIFIED DRUG; AKT1 PROTEIN, HUMAN; CARRIER PROTEIN; ENZYME INHIBITOR; GLYCOGEN; MUTANT PROTEIN; PAR6 PROTEIN, HUMAN; PAR6 PROTEIN, MOUSE; PHOSPHOTHREONINE; PKC 3 PROTEIN; PKC-3 PROTEIN; PROTEIN KINASE B; SIGNAL TRANSDUCING ADAPTOR PROTEIN;

ANIMAL CELL; ANIMAL TISSUE; ARTICLE; CONTROLLED STUDY; DELETION MUTANT; EMBRYO; ENZYME ACTIVATION; ENZYME ACTIVITY; ENZYME INHIBITION; ENZYME PHOSPHORYLATION; GLYCOGEN SYNTHESIS; HORMONAL REGULATION; HUMAN; HUMAN CELL; MOUSE; NONHUMAN; NUCLEOTIDE SEQUENCE; PH; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN INTERACTION; WILD TYPE; ANIMAL; BIOSYNTHESIS; C57BL MOUSE; CELL LINE; CHEMISTRY; DOWN REGULATION; DRUG ANTAGONISM; DRUG EFFECT; GENETICS; METABOLISM; PHOSPHORYLATION; PROTEIN BINDING; PROTEIN TERTIARY STRUCTURE;

ADAPTOR PROTEINS, SIGNAL TRANSDUCING; ANIMALS; CARRIER PROTEINS; CELL LINE; DOWN-REGULATION; ENZYME ACTIVATION; ENZYME INHIBITORS; GLYCOGEN; HUMANS; INSULIN; MICE; MICE, INBRED C57BL; MUTANT PROTEINS; PHOSPHORYLATION; PHOSPHOTHREONINE; PROTEIN BINDING; PROTEIN KINASE C; PROTEIN STRUCTURE, TERTIARY; PROTO-ONCOGENE PROTEINS C-AKT;

EID: 33947257824     PISSN: 03037207     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.mce.2007.01.011     Document Type: Article

References (30)

1. Adams J.M., Pratipanawatr T., Berria R., Wang E., DeFronzo R.A., Sullards M.C., and Mandarino L.J. Ceramide content is increased in skeletal muscle from obese insulin-resistant humans. Diabetes 53 1 (2004) 25-31
2. Bourbon N.A., Sandirasegarane L., and Kester M. Ceramide-induced inhibition of Akt is mediated through protein kinase Czeta: implications for growth arrest. J. Biol. Chem. 277 5 (2002) 3286-3292
3. Brazil D.P., Yang Z.Z., and Hemmings B.A. Advances in protein kinase B signalling: AKTion on multiple fronts. Trends Biochem. Sci. 29 5 (2004) 233-242
4. Cazzolli R., Carpenter L., Biden T.J., and Schmitz-Peiffer C. A role for protein phosphatase 2A-like activity, but not atypical protein kinase Czeta, in the inhibition of protein kinase B/Akt and glycogen synthesis by palmitate. Diabetes 50 10 (2001) 2210-2218
5. Chen C., and Okayama H. High-efficiency transformation of mammalian cells by plasmid DNA. Mol. Cell. Biol. 7 8 (1987) 2745-2752
6. Doornbos R.P., Theelen M., van der Hoeven P.C., van Blitterswijk W.J., Verkleij A.J., and van Bergen en Henegouwen P.M. Protein kinase Czeta is a negative regulator of protein kinase B activity. J. Biol. Chem. 274 13 (1999) 8589-8596
7. Etienne-Manneville S., and Hall A. Cdc42 regulates GSK-3beta and adenomatous polyposis coli to control cell polarity. Nature 421 6924 (2003) 753-756
8. Farese R.V., Sajan M.P., and Standaert M.L. Atypical protein kinase C in insulin action and insulin resistance. Biochem. Soc. Trans. 33 Pt 2 (2005) 350-353
9. Gao L., and Macara I.G. Isoforms of the polarity protein par6 have distinct functions. J. Biol. Chem. 279 40 (2004) 41557-41562
10. Hurd T.W., Gao L., Roh M.H., Macara I.G., and Margolis B. Direct interaction of two polarity complexes implicated in epithelial tight junction assembly. Nat. Cell Biol. 5 2 (2003) 137-142
11. Imai S., Kai M., Yamada K., Kanoh H., and Sakane F. The plasma membrane translocation of diacylglycerol kinase delta1 is negatively regulated by conventional protein kinase C-dependent phosphorylation at Ser-22 and Ser-26 within the pleckstrin homology domain. Biochem. J. 382 Pt 3 (2004) 957-966
12. Jensen J., Brennesvik E.O., Lai Y.C., and Shepherd P.R. GSK-3beta regulation in skeletal muscles by adrenaline and insulin: Evidence that PKA and PKB regulate different pools of GSK-3. Cell. Signal. 19 1 (2007) 204-210
13. Joberty G., Petersen C., Gao L., and Macara I.G. The cell-polarity protein Par6 links Par3 and atypical protein kinase C to Cdc42. Nat. Cell Biol. 2 8 (2000) 531-539
14. Johansson A., Driessens M., and Aspenstrom P. The mammalian homologue of the Caenorhabditis elegans polarity protein PAR-6 is a binding partner for the Rho GTPases Cdc42 and Rac1. J. Cell Sci. 113 Pt 18 (2000) 3267-3275
15. Kanzaki M., Mora S., Hwang J.B., Saltiel A.R., and Pessin J.E. Atypical protein kinase C (PKCζ/λ) is a convergent downstream target of the insulin-stimulated phosphatidylinositol 3-kinase and TC10 signaling pathways. J. Cell Biol. 164 2 (2004) 279-290
16. Liu Y.F., Paz K., Herschkovitz A., Alt A., Tennenbaum T., Sampson S.R., Ohba M., Kuroki T., LeRoith D., and Zick Y. Insulin stimulates PKCzeta-mediated phosphorylation of insulin receptor substrate-1 (IRS-1) A self-attenuated mechanism to negatively regulate the function of IRS proteins. J. Biol. Chem. 276 17 (2001) 14459-14465
17. Moeschel K., Beck A., Weigert C., Lammers R., Kalbacher H., Voelter W., Schleicher E.D., Haring H.U., and Lehmann R. Protein kinase C-zeta-induced phosphorylation of Ser318 in insulin receptor substrate-1 (IRS-1) attenuates the interaction with the insulin receptor and the tyrosine phosphorylation of IRS-1. J. Biol. Chem. 279 24 (2004) 25157-25163
18. Nawaratne R., Gray A., Jorgensen C.H., Downes C.P., Siddle K., and Sethi J.K. Regulation of insulin receptor substrate 1 pleckstrin homology domain by protein kinase C: role of serine 24 phosphorylation. Mol. Endocrinol. 20 8 (2006) 1838-1852
19. Noda Y., Kohjima M., Izaki T., Ota K., Yoshinaga S., Inagaki F., Ito T., and Sumimoto H. Molecular Recognition in Dimerization between PB1 Domains. J. Biol. Chem. 278 44 (2003) 43516-43524
20. Pear W.S., Nolan G.P., Scott M.L., and Baltimore D. Production of high-titer helper-free retroviruses by transient transfection. Proc. Natl. Acad. Sci. U.S.A. 90 18 (1993) 8392-8396
21. Plant P.J., Fawcett J.P., Lin D.C., Holdorf A.D., Binns K., Kulkarni S., and Pawson T. A polarity complex of mPar-6 and atypical PKC binds, phosphorylates and regulates mammalian Lgl. Nat. Cell Biol. 5 4 (2003) 301-308
22. Powell D.J., Hajduch E., Kular G., and Hundal H.S. Ceramide disables 3-phosphoinositide binding to the pleckstrin homology domain of protein kinase B (PKB)/Akt by a PKCzeta-dependent mechanism. Mol. Cell. Biol. 23 21 (2003) 7794-7808
23. Powell D.J., Turban S., Gray A., Hajduch E., and Hundal H.S. Intracellular ceramide synthesis and protein kinase Czeta activation play an essential role in palmitate-induced insulin resistance in rat L6 skeletal muscle cells. Biochem. J. 382 Pt 2 (2004) 619-629
24. Ravichandran L.V., Esposito D.L., Chen J., and Quon M.J. Protein kinase C-zeta phosphorylates insulin receptor substrate-1 and impairs its ability to activate phosphatidylinositol 3-kinase in response to insulin. J. Biol. Chem. 276 5 (2001) 3543-3549
25. Standaert M.L., Bandyopadhyay G., Kanoh Y., Sajan M.P., and Farese R.V. Insulin and PIP3 activate PKC-zeta by mechanisms that are both dependent and independent of phosphorylation of activation loop (T410) and autophosphorylation (T560) sites. Biochemistry 40 1 (2001) 249-255
26. Summers S.A., and Nelson D.H. A role for sphingolipids in producing the common features of type 2 diabetes, metabolic syndrome X, and Cushing's syndrome. Diabetes 54 3 (2005) 591-602
27. Weyrich P., Kapp K., Niederfellner G., Melzer M., Lehmann R., Haring H.U., and Lammers R. Partitioning-defective protein 6 regulates insulin-dependent glycogen synthesis via atypical protein kinase C. Mol. Endocrinol. 18 5 (2004) 1287-1300
28. Weyrich P., Lammers R., Fritsche A., Machicao F., Haring H.U., and Stefan N. A novel functional polymorphism (-336A/G) in the promoter of the partitioning-defective protein-6alpha gene is associated with increased glucose tolerance and lower concentrations of serum non-esterified fatty acids. Diabetologia 48 4 (2005) 669-674
29. Yamanaka T., Horikoshi Y., Suzuki A., Sugiyama Y., Kitamura K., Maniwa R., Nagai Y., Yamashita A., Hirose T., Ishikawa H., and Ohno S. PAR-6 regulates aPKC activity in a novel way and mediates cell-cell contact-induced formation of the epithelial junctional complex. Genes Cells 6 8 (2001) 721-731
30. Zick Y. Uncoupling insulin signalling by serine/threonine phosphorylation: a molecular basis for insulin resistance. Biochem. Soc. Trans. 32 Pt 5 (2004) 812-816