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Volumn 18, Issue 5, 2004, Pages 1287-1300

Partitioning-defective protein 6 regulates insulin-dependent glycogen synthesis via atypical protein kinase C

Author keywords

[No Author keywords available]

Indexed keywords

GLYCOGEN SYNTHASE KINASE 3ALPHA; GLYCOGEN SYNTHASE KINASE 3BETA; INSULIN; INSULIN RECEPTOR SUBSTRATE 1; PARTITIONING DEFECTIVE PROTEIN 6; PHOSPHATIDYLINOSITOL 3 KINASE; PLATELET DERIVED GROWTH FACTOR; PROTEIN INTERACTING WITH PROTEIN KINASE C; PROTEIN KINASE B; PROTEIN KINASE C; PROTEIN P85; PROTEIN SUBUNIT; UNCLASSIFIED DRUG;

EID: 2342478591     PISSN: 08888809     EISSN: None     Source Type: Journal    
DOI: 10.1210/me.2003-0253     Document Type: Article
Times cited : (7)

References (73)
  • 2
    • 0027977927 scopus 로고
    • A role for zeta protein kinase C in nerve growth factor-induced differentiation of PC12 cells
    • Wooten MW, Zhou G, Seibenhener ML, Coleman ES 1994 A role for zeta protein kinase C in nerve growth factor-induced differentiation of PC12 cells. Cell Growth Differ 5:395-403
    • (1994) Cell Growth Differ , vol.5 , pp. 395-403
    • Wooten, M.W.1    Zhou, G.2    Seibenhener, M.L.3    Coleman, E.S.4
  • 3
    • 0035807836 scopus 로고    scopus 로고
    • Bazooka and atypical protein kinase C are required to regulate oocyte differentiation in the Drosophila ovary
    • Cox DN, Seyfried SA, Jan LY, Jan YN 2001 Bazooka and atypical protein kinase C are required to regulate oocyte differentiation in the Drosophila ovary. Proc Natl Acad Sci USA 98:14475-14480
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 14475-14480
    • Cox, D.N.1    Seyfried, S.A.2    Jan, L.Y.3    Jan, Y.N.4
  • 4
    • 0030792007 scopus 로고    scopus 로고
    • Positioning atypical protein kinase C isoforms in the UV-induced apoptotic signaling cascade
    • Berra E, Municio MM, Sanz L, Frutos S, Diaz-Meco MT, Moscat J 1997 Positioning atypical protein kinase C isoforms in the UV-induced apoptotic signaling cascade. Mol Cell Biol 17:4346-4354
    • (1997) Mol Cell Biol , vol.17 , pp. 4346-4354
    • Berra, E.1    Municio, M.M.2    Sanz, L.3    Frutos, S.4    Diaz-Meco, M.T.5    Moscat, J.6
  • 6
    • 0033621957 scopus 로고    scopus 로고
    • Atypical protein kinases Cλ and -ζ associate with the GTP-binding protein Cdc42 and mediate stress fiber loss
    • Coghlan MP, Chou MM, Carpenter CL 2000 Atypical protein kinases Cλ and -ζ associate with the GTP-binding protein Cdc42 and mediate stress fiber loss. Mol Cell Biol 20:2880-2889
    • (2000) Mol Cell Biol , vol.20 , pp. 2880-2889
    • Coghlan, M.P.1    Chou, M.M.2    Carpenter, C.L.3
  • 7
    • 0031674842 scopus 로고    scopus 로고
    • Atypical protein kinase C cooperates with PAR-3 to establish embryonic polarity in Caenorhabditis elegans
    • Tabuse Y, Izumi Y, Piano F, Kemphues KJ, Miwa J, Ohno S 1998 Atypical protein kinase C cooperates with PAR-3 to establish embryonic polarity in Caenorhabditis elegans. Development 125:3607-3614
    • (1998) Development , vol.125 , pp. 3607-3614
    • Tabuse, Y.1    Izumi, Y.2    Piano, F.3    Kemphues, K.J.4    Miwa, J.5    Ohno, S.6
  • 8
    • 0036828968 scopus 로고    scopus 로고
    • Regulated protein-protein interaction between aPKC and PAR-3 plays an essential role in the polarization of epithelial cells
    • Nagai-Tamai Y, Mizuno K, Hirose T, Suzuki A, Ohno S 2002 Regulated protein-protein interaction between aPKC and PAR-3 plays an essential role in the polarization of epithelial cells. Genes Cells 7:1161-1171
    • (2002) Genes Cells , vol.7 , pp. 1161-1171
    • Nagai-Tamai, Y.1    Mizuno, K.2    Hirose, T.3    Suzuki, A.4    Ohno, S.5
  • 9
    • 0032487494 scopus 로고    scopus 로고
    • An atypical PKC directly associates and colocalizes at the epithelial tight junction with ASIP, a mammalian homologue of Caenorhabditis elegans polarity protein PAR-3
    • Izumi Y, Hirose T, Tamai Y, Hirai S, Nagashima Y, Fujimoto T, Tabuse Y, Kemphues KJ, Ohno S 1998 An atypical PKC directly associates and colocalizes at the epithelial tight junction with ASIP, a mammalian homologue of Caenorhabditis elegans polarity protein PAR-3. J Cell Biol 143:95-106
    • (1998) J Cell Biol , vol.143 , pp. 95-106
    • Izumi, Y.1    Hirose, T.2    Tamai, Y.3    Hirai, S.4    Nagashima, Y.5    Fujimoto, T.6    Tabuse, Y.7    Kemphues, K.J.8    Ohno, S.9
  • 10
    • 0035911955 scopus 로고    scopus 로고
    • Atypical protein kinase C is involved in the evolutionarily conserved par protein complex and plays a critical role in establishing epithelia-specific junctional structures
    • Suzuki A, Yamanaka T, Hirose T, Manabe N, Mizuno K, Shimizu M, Akimoto K, Izumi Y, Ohnishi T, Ohno S 2001 Atypical protein kinase C is involved in the evolutionarily conserved par protein complex and plays a critical role in establishing epithelia-specific junctional structures. J Cell Biol 152:1183-1196
    • (2001) J Cell Biol , vol.152 , pp. 1183-1196
    • Suzuki, A.1    Yamanaka, T.2    Hirose, T.3    Manabe, N.4    Mizuno, K.5    Shimizu, M.6    Akimoto, K.7    Izumi, Y.8    Ohnishi, T.9    Ohno, S.10
  • 11
    • 0036288402 scopus 로고    scopus 로고
    • Function and dysfunction of aPKC isoforms for glucose transport in insulin-sensitive and insulin-resistant states
    • Farese RV 2002 Function and dysfunction of aPKC isoforms for glucose transport in insulin-sensitive and insulin-resistant states. Am J Physiol Endocrinol Metab 283:E1-E11
    • (2002) Am J Physiol Endocrinol Metab , vol.283
    • Farese, R.V.1
  • 12
    • 0030812546 scopus 로고    scopus 로고
    • Evidence for involvement of protein kinase C (PKC)-ζ and noninvolvement of diacylglycerol-sensitive PKCs in insulin-stimulated glucose transport in L6 myotubes
    • Bandyopadhyay G, Standaert ML, Galloway L, Moscat J, Farese RV 1997 Evidence for involvement of protein kinase C (PKC)-ζ and noninvolvement of diacylglycerol-sensitive PKCs in insulin-stimulated glucose transport in L6 myotubes. Endocrinology 138:4721-4731
    • (1997) Endocrinology , vol.138 , pp. 4721-4731
    • Bandyopadhyay, G.1    Standaert, M.L.2    Galloway, L.3    Moscat, J.4    Farese, R.V.5
  • 14
    • 0036225280 scopus 로고    scopus 로고
    • Cbl, IRS-1, and IRS-2 mediate effects of rosiglitazone on PI3K, PKC-λ, and glucose transport in 3T3/L1 adipocytes
    • Standaert ML, Kanoh Y, Sajan MP, Bandyopadhyay G, Farese RV 2002 Cbl, IRS-1, and IRS-2 mediate effects of rosiglitazone on PI3K, PKC-λ, and glucose transport in 3T3/L1 adipocytes. Endocrinology 143:1705-1716
    • (2002) Endocrinology , vol.143 , pp. 1705-1716
    • Standaert, M.L.1    Kanoh, Y.2    Sajan, M.P.3    Bandyopadhyay, G.4    Farese, R.V.5
  • 15
    • 0033695810 scopus 로고    scopus 로고
    • Effects of adenoviral gene transfer of wild-type, constitutively active, and kinase-defective protein kinase C-λ on insulin-stimulated glucose transport in L6 myotubes
    • Bandyopadhyay G, Kanoh Y, Sajan MP, Standaert ML, Farese RV 2000 Effects of adenoviral gene transfer of wild-type, constitutively active, and kinase-defective protein kinase C-λ on insulin-stimulated glucose transport in L6 myotubes. Endocrinology 141:4120-4127
    • (2000) Endocrinology , vol.141 , pp. 4120-4127
    • Bandyopadhyay, G.1    Kanoh, Y.2    Sajan, M.P.3    Standaert, M.L.4    Farese, R.V.5
  • 16
    • 0033082749 scopus 로고    scopus 로고
    • Effects of transiently expressed atypical (ζ, λ), conventional (α, β) and novel (δ, ε) protein kinase C isoforms on insulin-stimulated translocation of epitope-tagged GLUT4 glucose transporters in rat adipocytes: Specific interchangeable effects of protein kinases C-ζ and C-λ
    • Bandyopadhyay G, Standaert ML, Kikkawa U, Ono Y, Moscat J, Farese RV 1999 Effects of transiently expressed atypical (ζ, λ), conventional (α, β) and novel (δ, ε) protein kinase C isoforms on insulin-stimulated translocation of epitope-tagged GLUT4 glucose transporters in rat adipocytes: specific interchangeable effects of protein kinases C-ζ and C-λ. Biochem J 337:461-470
    • (1999) Biochem J , vol.337 , pp. 461-470
    • Bandyopadhyay, G.1    Standaert, M.L.2    Kikkawa, U.3    Ono, Y.4    Moscat, J.5    Farese, R.V.6
  • 17
    • 0031038052 scopus 로고    scopus 로고
    • Activation of protein kinase C (α, β, and ζ) by insulin in 3T3/L1 cells. Transfection studies suggest a role for PKC-ζ in glucose transport
    • Bandyopadhyay G, Standaert ML, Zhao L, Yu B, Avignon A, Galloway L, Karnam P, Moscat J, Farese RV 1997 Activation of protein kinase C (α, β, and ζ) by insulin in 3T3/L1 cells. Transfection studies suggest a role for PKC-ζ in glucose transport. J Biol Chem 272:2551-2558
    • (1997) J Biol Chem , vol.272 , pp. 2551-2558
    • Bandyopadhyay, G.1    Standaert, M.L.2    Zhao, L.3    Yu, B.4    Avignon, A.5    Galloway, L.6    Karnam, P.7    Moscat, J.8    Farese, R.V.9
  • 19
    • 0034774069 scopus 로고    scopus 로고
    • Activation of protein kinase Cζ induces serine phosphorylation of vamp2 in the glut4 compartment and increases glucose transport in skeletal muscle
    • Braiman L, Alt A, Kuroki T, Ohba M, Bak A, Tennenbaum T, Sampson SR 2001 Activation of protein kinase Cζ induces serine phosphorylation of vamp2 in the glut4 compartment and increases glucose transport in skeletal muscle. Mol Cell Biol 21:7852-7861
    • (2001) Mol Cell Biol , vol.21 , pp. 7852-7861
    • Braiman, L.1    Alt, A.2    Kuroki, T.3    Ohba, M.4    Bak, A.5    Tennenbaum, T.6    Sampson, S.R.7
  • 20
    • 0035957949 scopus 로고    scopus 로고
    • Insulin stimulates PKCζ-mediated phosphorylation of insulin receptor substrate-1 (IRS-1). A self-attenuated mechanism to negatively regulate the function of IRS proteins
    • Liu YF, Paz K, Herschkovitz A, Alt A, Tennenbaum T, Sampson SR, Ohba M, Kuroki T, LeRoith D, Zick Y 2001 Insulin stimulates PKCζ-mediated phosphorylation of insulin receptor substrate-1 (IRS-1). A self-attenuated mechanism to negatively regulate the function of IRS proteins. J Biol Chem 276:14459-14465
    • (2001) J Biol Chem , vol.276 , pp. 14459-14465
    • Liu, Y.F.1    Paz, K.2    Herschkovitz, A.3    Alt, A.4    Tennenbaum, T.5    Sampson, S.R.6    Ohba, M.7    Kuroki, T.8    LeRoith, D.9    Zick, Y.10
  • 21
    • 0035793592 scopus 로고    scopus 로고
    • Protein kinase C-ζ phosphorylates insulin receptor substrate-1 and impairs its ability to activate phosphatidylinositol 3-kinase in response to insulin
    • Ravichandran LV, Esposito DL, Chen J, Quon MJ 2001 Protein kinase C-ζ phosphorylates insulin receptor substrate-1 and impairs its ability to activate phosphatidylinositol 3-kinase in response to insulin. J Biol Chem 276:3543-3549
    • (2001) J Biol Chem , vol.276 , pp. 3543-3549
    • Ravichandran, L.V.1    Esposito, D.L.2    Chen, J.3    Quon, M.J.4
  • 22
    • 0035896366 scopus 로고    scopus 로고
    • Protein kinase B (PKB/Akt) - A key regulator of glucose transport?
    • Hajduch E, Litherland GJ, Hundal HS 2001 Protein kinase B (PKB/Akt) - a key regulator of glucose transport? FEBS Lett 492:199-203
    • (2001) FEBS Lett , vol.492 , pp. 199-203
    • Hajduch, E.1    Litherland, G.J.2    Hundal, H.S.3
  • 23
    • 0034845958 scopus 로고    scopus 로고
    • PKB/Akt: A key mediator of cell proliferation, survival and insulin responses?
    • Lawlor MA, Alessi DR 2001 PKB/Akt: a key mediator of cell proliferation, survival and insulin responses? J Cell Sci 114:2903-2910
    • (2001) J Cell Sci , vol.114 , pp. 2903-2910
    • Lawlor, M.A.1    Alessi, D.R.2
  • 24
    • 0031127305 scopus 로고    scopus 로고
    • Characterization of a 3-phosphoinositide-dependent protein kinase which phosphorylates and activates protein kinase Bα
    • Alessi DR, James SR, Downes CP, Holmes AB, Gaffney PR, Reese CB, Cohen P 1997 Characterization of a 3-phosphoinositide-dependent protein kinase which phosphorylates and activates protein kinase Bα. Curr Biol 7:261-269
    • (1997) Curr Biol , vol.7 , pp. 261-269
    • Alessi, D.R.1    James, S.R.2    Downes, C.P.3    Holmes, A.B.4    Gaffney, P.R.5    Reese, C.B.6    Cohen, P.7
  • 25
    • 0028670203 scopus 로고
    • The pleckstrin homology domain of RAC protein kinase associates with the regulatory domain of protein kinase C ζ
    • Konishi H, Kuroda S, Kikkawa U 1994 The pleckstrin homology domain of RAC protein kinase associates with the regulatory domain of protein kinase C ζ. Biochem Biophys Res Commun 205:1770-1775
    • (1994) Biochem Biophys Res Commun , vol.205 , pp. 1770-1775
    • Konishi, H.1    Kuroda, S.2    Kikkawa, U.3
  • 27
    • 0034533061 scopus 로고    scopus 로고
    • Inhibition of growth-factor-induced phosphorylation and activation of protein kinase B/Akt by atypical protein kinase C in breast cancer cells
    • Mao M, Fang X, Lu Y, Lapushin R, Bast RC, Mills GB 2000 Inhibition of growth-factor-induced phosphorylation and activation of protein kinase B/Akt by atypical protein kinase C in breast cancer cells. Biochem J 352(Pt 2):475-482
    • (2000) Biochem J , vol.352 , Issue.2 PART , pp. 475-482
    • Mao, M.1    Fang, X.2    Lu, Y.3    Lapushin, R.4    Bast, R.C.5    Mills, G.B.6
  • 28
    • 0029933665 scopus 로고    scopus 로고
    • Tumor necrosis factor (TNF)-α inhibits insulin signaling through stimulation of the p55 TNF receptor and activation of sphingomyellnase
    • Peraldi P, Hotamisligil GS, Buurman WA, White MF, Spiegelman BM 1996 Tumor necrosis factor (TNF)-α inhibits insulin signaling through stimulation of the p55 TNF receptor and activation of sphingomyellnase. J Biol Chem 271:13018-13022
    • (1996) J Biol Chem , vol.271 , pp. 13018-13022
    • Peraldi, P.1    Hotamisligil, G.S.2    Buurman, W.A.3    White, M.F.4    Spiegelman, B.M.5
  • 29
    • 0038532298 scopus 로고    scopus 로고
    • A role for ceramide, but not diacylglycerol, in the antagonism of insulin signal transduction by saturated fatty acids
    • Chavez JA, Knotts TA, Wang LP, Li G, Dobrowsky RT, Florant GL, Summers SA 2003 A role for ceramide, but not diacylglycerol, in the antagonism of insulin signal transduction by saturated fatty acids. J Biol Chem 278:10297-10303
    • (2003) J Biol Chem , vol.278 , pp. 10297-10303
    • Chavez, J.A.1    Knotts, T.A.2    Wang, L.P.3    Li, G.4    Dobrowsky, R.T.5    Florant, G.L.6    Summers, S.A.7
  • 30
    • 0031841949 scopus 로고    scopus 로고
    • Regulation of insulin-stimulated glucose transporter GLUT4 translocation and Akt kinase activity by ceramide
    • Summers SA, Garza LA Zhou H, Bimbaum MJ 1998 Regulation of insulin-stimulated glucose transporter GLUT4 translocation and Akt kinase activity by ceramide. Mol Cell Biol 18:5457-5464
    • (1998) Mol Cell Biol , vol.18 , pp. 5457-5464
    • Summers, S.A.1    Garza, L.A.2    Zhou, H.3    Bimbaum, M.J.4
  • 31
    • 0035513703 scopus 로고    scopus 로고
    • Ceramide mediates insulin resistance by tumor necrosis factor-α in brown adipocytes by maintaining Akt in an inactive dephosphorylated state
    • Teruel T, Hernandez R, Lorenzo M 2001 Ceramide mediates insulin resistance by tumor necrosis factor-α in brown adipocytes by maintaining Akt in an inactive dephosphorylated state. Diabetes 50:2563-2571
    • (2001) Diabetes , vol.50 , pp. 2563-2571
    • Teruel, T.1    Hernandez, R.2    Lorenzo, M.3
  • 32
    • 0035133331 scopus 로고    scopus 로고
    • Ceramide impairs the insulin-dependent membrane recruitment of protein kinase B leading to a loss in downstream signalling in L6 skeletal muscle cells
    • Hajduch E, Balendran A, Batty IH, Litherland GJ, Blair AS, Downes CP, Hundal HS 2001 Ceramide impairs the insulin-dependent membrane recruitment of protein kinase B leading to a loss in downstream signalling in L6 skeletal muscle cells. Diabetologia 44:173-183
    • (2001) Diabetologia , vol.44 , pp. 173-183
    • Hajduch, E.1    Balendran, A.2    Batty, I.H.3    Litherland, G.J.4    Blair, A.S.5    Downes, C.P.6    Hundal, H.S.7
  • 33
    • 0036479251 scopus 로고    scopus 로고
    • Ceramide-induced inhibition of Akt is mediated through protein kinase Cζ: Implications for growth arrest
    • Bourbon NA, Sandirasegarane L, Kester M 2002 Ceramide-induced inhibition of Akt is mediated through protein kinase Cζ: implications for growth arrest. J Biol Chem 277:3286-3292
    • (2002) J Biol Chem , vol.277 , pp. 3286-3292
    • Bourbon, N.A.1    Sandirasegarane, L.2    Kester, M.3
  • 34
    • 0034634596 scopus 로고    scopus 로고
    • Ceramide directly activates protein kinase Cζ to regulate a stress-activated protein kinase signaling complex
    • Bourbon NA, Yun J, Kester M 2000 Ceramide directly activates protein kinase Cζ to regulate a stress-activated protein kinase signaling complex. J Biol Chem 275:35617-35623
    • (2000) J Biol Chem , vol.275 , pp. 35617-35623
    • Bourbon, N.A.1    Yun, J.2    Kester, M.3
  • 35
    • 0033081893 scopus 로고    scopus 로고
    • Atypical PKC ζ is activated by ceramide, resulting in coactivation of NF-κB/JNK kinase and cell survival
    • Wang YM, Selbenhener ML, Vandenplas ML, Wooten MW 1999 Atypical PKC ζ is activated by ceramide, resulting In coactivation of NF-κB/JNK kinase and cell survival. J Neurosci Res 55:293-302
    • (1999) J Neurosci Res , vol.55 , pp. 293-302
    • Wang, Y.M.1    Selbenhener, M.L.2    Vandenplas, M.L.3    Wooten, M.W.4
  • 36
    • 0029850113 scopus 로고    scopus 로고
    • Par-6, a gene involved in the establishment of asymmetry in early C. elegans embryos, mediates the asymmetric localization of PAR-3
    • Watts JL, Etemad-Moghadam B, Guo S, Boyd L, Draper BW, Mello CC, Priess JR, Kemphues KJ 1996 Par-6, a gene involved in the establishment of asymmetry in early C. elegans embryos, mediates the asymmetric localization of PAR-3. Development 122:3133-3140
    • (1996) Development , vol.122 , pp. 3133-3140
    • Watts, J.L.1    Etemad-Moghadam, B.2    Guo, S.3    Boyd, L.4    Draper, B.W.5    Mello, C.C.6    Priess, J.R.7    Kemphues, K.J.8
  • 37
    • 0035141027 scopus 로고    scopus 로고
    • DmPAR-6 directs epithelial polarity and asymmetric cell division of neuroblasts in Drosophila
    • Petronczki M, Knoblich JA 2001 DmPAR-6 directs epithelial polarity and asymmetric cell division of neuroblasts in Drosophila. Nat Cell Biol 3:43-49
    • (2001) Nat Cell Biol , vol.3 , pp. 43-49
    • Petronczki, M.1    Knoblich, J.A.2
  • 38
    • 0035811044 scopus 로고    scopus 로고
    • Bazooka and PAR-6 are required with PAR-1 for the maintenance of oocyte fate in Drosophila
    • Huynh JR, Petronczki M, Knoblich JA, St Johnston D 2001 Bazooka and PAR-6 are required with PAR-1 for the maintenance of oocyte fate in Drosophila. Curr Biol 11:901-906
    • (2001) Curr Biol , vol.11 , pp. 901-906
    • Huynh, J.R.1    Petronczki, M.2    Knoblich, J.A.3    St Johnston, D.4
  • 39
    • 0037022122 scopus 로고    scopus 로고
    • Assembly of epithelial tight junctions is negatively regulated by Par6
    • Gao L, Joberty G, Macara IG 2002 Assembly of epithelial tight junctions is negatively regulated by Par6. Curr Biol 12:221-225
    • (2002) Curr Biol , vol.12 , pp. 221-225
    • Gao, L.1    Joberty, G.2    Macara, I.G.3
  • 40
    • 0034253536 scopus 로고    scopus 로고
    • The cell-polarity protein Par6 links Par3 and atypical protein kinase C to Cdc42
    • Joberty G, Petersen C, Gao L, Macara IG 2000 The cell-polarity protein Par6 links Par3 and atypical protein kinase C to Cdc42. Nat Cell Biol 2:531-539
    • (2000) Nat Cell Biol , vol.2 , pp. 531-539
    • Joberty, G.1    Petersen, C.2    Gao, L.3    Macara, I.G.4
  • 41
    • 0034659420 scopus 로고    scopus 로고
    • A human homolog of the C. elegans polarity determinant Par-6 links Rac and Cdc42 to PKCζ signaling and cell transformation
    • Qiu RG, Abo A, Steven Martin G 2000 A human homolog of the C. elegans polarity determinant Par-6 links Rac and Cdc42 to PKCζ signaling and cell transformation. Curr Biol 10:697-707
    • (2000) Curr Biol , vol.10 , pp. 697-707
    • Qiu, R.G.1    Abo, A.2    Steven Martin, G.3
  • 42
    • 0035070099 scopus 로고    scopus 로고
    • Human homologues of the Caenorhabditis elegans cell polarity protein PAR6 as an adaptor that links the small GTPases Rac and Cdc42 to atypical protein kinase C
    • Noda Y, Takeya R, Ohno S, Naito S, Ito T, Sumimoto H 2001 Human homologues of the Caenorhabditis elegans cell polarity protein PAR6 as an adaptor that links the small GTPases Rac and Cdc42 to atypical protein kinase C. Genes Cells 6:107-119
    • (2001) Genes Cells , vol.6 , pp. 107-119
    • Noda, Y.1    Takeya, R.2    Ohno, S.3    Naito, S.4    Ito, T.5    Sumimoto, H.6
  • 44
    • 0038313002 scopus 로고    scopus 로고
    • Identification of an in vitro insulin receptor substrate-1 phosphorylation site by negative-ion muLC/ES-API-CID-MS hybrid scan technique
    • Beck A, Moeschel K, Deeg M, Haring HU, Voelter W, Schleicher ED, Lehmann R 2003 Identification of an in vitro insulin receptor substrate-1 phosphorylation site by negative-ion muLC/ES-API-CID-MS hybrid scan technique. J Am Soc Mass Spectrom 14:401-405
    • (2003) J Am Soc Mass Spectrom , vol.14 , pp. 401-405
    • Beck, A.1    Moeschel, K.2    Deeg, M.3    Haring, H.U.4    Voelter, W.5    Schleicher, E.D.6    Lehmann, R.7
  • 45
    • 0037631323 scopus 로고    scopus 로고
    • Activation of Raf-1 signaling by protein kinase C through a mechanism involving Raf kinase inhibitory protein
    • Corbit KC, Trakul N, Eves EM, Diaz B, Marshall M, Rosner MR 2003 Activation of Raf-1 signaling by protein kinase C through a mechanism involving Raf kinase inhibitory protein. J Biol Chem 278:13061-13068
    • (2003) J Biol Chem , vol.278 , pp. 13061-13068
    • Corbit, K.C.1    Trakul, N.2    Eves, E.M.3    Diaz, B.4    Marshall, M.5    Rosner, M.R.6
  • 46
    • 0033607633 scopus 로고    scopus 로고
    • Phosphorylation and regulation of Raf by Akt (protein kinase B)
    • Zimmermann S, Moelling K 1999 Phosphorylation and regulation of Raf by Akt (protein kinase B). Science 286:1741-1744
    • (1999) Science , vol.286 , pp. 1741-1744
    • Zimmermann, S.1    Moelling, K.2
  • 48
    • 0034710617 scopus 로고    scopus 로고
    • Cell polarity: Scaffold proteins par excellence
    • Brazil DP, Hemmings BA 2000 Cell polarity: scaffold proteins par excellence. Curr Biol 10:R592-R594
    • (2000) Curr Biol , vol.10
    • Brazil, D.P.1    Hemmings, B.A.2
  • 49
    • 0037434790 scopus 로고    scopus 로고
    • Cdc42 regulates GSK-3β and adenomatous polyposis coli to control cell polarity
    • Etienne-Manneville S, Hall A 2003 Cdc42 regulates GSK-3β and adenomatous polyposis coli to control cell polarity. Nature 421:753-756
    • (2003) Nature , vol.421 , pp. 753-756
    • Etienne-Manneville, S.1    Hall, A.2
  • 50
    • 0033588253 scopus 로고    scopus 로고
    • Ceramide generation is sufficient to account for the inhibition of the insulin-stimulated PKB pathway in C2C12 skeletal muscle cells pretreated with palmitate
    • Schmitz-Peiffer C, Craig DL, Biden TJ 1999 Ceramide generation is sufficient to account for the inhibition of the insulin-stimulated PKB pathway in C2C12 skeletal muscle cells pretreated with palmitate. J Biol Chem 274:24202-24210
    • (1999) J Biol Chem , vol.274 , pp. 24202-24210
    • Schmitz-Peiffer, C.1    Craig, D.L.2    Biden, T.J.3
  • 51
    • 0025123408 scopus 로고
    • 1,2-Diacylglycerol and ceramide levels in insulin-resistant tissues of the rat in vivo
    • Turinsky J, O'Sullivan DM, Bayly BP 1990 1,2-Diacylglycerol and ceramide levels in insulin-resistant tissues of the rat in vivo. J Biol Chem 265:16880-16885
    • (1990) J Biol Chem , vol.265 , pp. 16880-16885
    • Turinsky, J.1    O'Sullivan, D.M.2    Bayly, B.P.3
  • 52
    • 0032569026 scopus 로고    scopus 로고
    • Inhibition of Akt kinase by cell-permeable ceramide and its implications for ceramide-induced apoptosis
    • Zhou H, Summers SA, Bimbaum MJ, Pittman RN 1998 Inhibition of Akt kinase by cell-permeable ceramide and its implications for ceramide-induced apoptosis. J Biol Chem 273:16568-16575
    • (1998) J Biol Chem , vol.273 , pp. 16568-16575
    • Zhou, H.1    Summers, S.A.2    Bimbaum, M.J.3    Pittman, R.N.4
  • 53
    • 0037059330 scopus 로고    scopus 로고
    • Phosphorylation of Ser307 in IRS-1 blocks interactions with the insulin receptor and inhibits insulin action
    • Aguirre V, Werner ED, Giraud J, Lee YH, Shoelson SE, White MF 2002 Phosphorylation of Ser307 in IRS-1 blocks interactions with the insulin receptor and inhibits insulin action. J Biol Chem 277:1531-1537
    • (2002) J Biol Chem , vol.277 , pp. 1531-1537
    • Aguirre, V.1    Werner, E.D.2    Giraud, J.3    Lee, Y.H.4    Shoelson, S.E.5    White, M.F.6
  • 54
    • 0030669392 scopus 로고    scopus 로고
    • A molecular basis for insulin resistance. Elevated serine/threonine phosphorylation of IRS-1 and IRS-2 inhibits their binding to the juxtamembrane region of the insulin receptor and impairs their ability to undergo insulin-induced tyrosine phosphorylation
    • Paz K, Hemi R, LeRoith D, Karasik A, Elhanany E, Kanety H, Zick Y 1997 A molecular basis for insulin resistance. Elevated serine/threonine phosphorylation of IRS-1 and IRS-2 inhibits their binding to the juxtamembrane region of the insulin receptor and impairs their ability to undergo insulin-induced tyrosine phosphorylation. J Biol Chem 272:29911-29918
    • (1997) J Biol Chem , vol.272 , pp. 29911-29918
    • Paz, K.1    Hemi, R.2    LeRoith, D.3    Karasik, A.4    Elhanany, E.5    Kanety, H.6    Zick, Y.7
  • 55
    • 0030669094 scopus 로고    scopus 로고
    • Protein kinase C modulation of insulin receptor substrate-1 tyrosine phosphorylation requires serine 612
    • De Fea K, Roth RA 1997 Protein kinase C modulation of insulin receptor substrate-1 tyrosine phosphorylation requires serine 612. Biochemistry 36:12939-12947
    • (1997) Biochemistry , vol.36 , pp. 12939-12947
    • De Fea, K.1    Roth, R.A.2
  • 56
    • 15844389443 scopus 로고    scopus 로고
    • Phosphorylation of insulin receptor substrate-1 on multiple serine residues, 612, 632, 662, and 731, modulates insulin action
    • Mothe I, Van Obberghen E 1996 Phosphorylation of insulin receptor substrate-1 on multiple serine residues, 612, 632, 662, and 731, modulates insulin action. J Biol Chem 271:11222-11227
    • (1996) J Biol Chem , vol.271 , pp. 11222-11227
    • Mothe, I.1    Van Obberghen, E.2
  • 57
    • 0030061922 scopus 로고    scopus 로고
    • IRS-1-mediated inhibition of insulin receptor tyrosine kinase activity in TNF-α- and obesity-induced insulin resistance
    • Hotamisligil GS, Peraldi P, Budavari A, Ellis R, White MF, Spiegelman BM 1996 IRS-1-mediated inhibition of insulin receptor tyrosine kinase activity in TNF-α- and obesity-induced insulin resistance. Science 271:665-668
    • (1996) Science , vol.271 , pp. 665-668
    • Hotamisligil, G.S.1    Peraldi, P.2    Budavari, A.3    Ellis, R.4    White, M.F.5    Spiegelman, B.M.6
  • 58
    • 0033600924 scopus 로고    scopus 로고
    • JAK1-dependent phosphorylation of insulin receptor substrate-1 (IRS-1) is inhibited by IRS-1 serine phosphorylation
    • Cengel KA, Freund GG 1999 JAK1-dependent phosphorylation of insulin receptor substrate-1 (IRS-1) is inhibited by IRS-1 serine phosphorylation. J Biol Chem 274:27969-27974
    • (1999) J Biol Chem , vol.274 , pp. 27969-27974
    • Cengel, K.A.1    Freund, G.G.2
  • 59
    • 0042421854 scopus 로고    scopus 로고
    • Platelet-derived growth factor (PDGF) stimulates glucose transport in 3T3-L1 adipocytes overexpressing PDGF receptor by a pathway independent of insulin receptor substrates
    • Whiteman EL, Chen JJ, Birnbaum MJ 2003 Platelet-derived growth factor (PDGF) stimulates glucose transport In 3T3-L1 adipocytes overexpressing PDGF receptor by a pathway independent of insulin receptor substrates. Endocrinology 144:3811-3820
    • (2003) Endocrinology , vol.144 , pp. 3811-3820
    • Whiteman, E.L.1    Chen, J.J.2    Birnbaum, M.J.3
  • 60
    • 0142091454 scopus 로고    scopus 로고
    • Ceramide disables 3-phosphoinositide binding to the pleckstrin homology domain of protein kinase B (PKB)/Akt by a PKCζ-dependent mechanism
    • Powell DJ, Hajduch E, Kular G, Hundal HS 2003 Ceramide disables 3-phosphoinositide binding to the pleckstrin homology domain of protein kinase B (PKB)/Akt by a PKCζ-dependent mechanism. Mol Cell Biol 23:7794-7808
    • (2003) Mol Cell Biol , vol.23 , pp. 7794-7808
    • Powell, D.J.1    Hajduch, E.2    Kular, G.3    Hundal, H.S.4
  • 61
    • 0035487315 scopus 로고    scopus 로고
    • A role for protein phosphatase 2A-like activity, but not atypical protein kinase Cζ, in the inhibition of protein kinase B/Akt and glycogen synthesis by palmitate
    • Cazzolli R, Carpenter L, Biden TJ, Schmitz-Peiffer C 2001 A role for protein phosphatase 2A-like activity, but not atypical protein kinase Cζ, in the inhibition of protein kinase B/Akt and glycogen synthesis by palmitate. Diabetes 50:2210-2218
    • (2001) Diabetes , vol.50 , pp. 2210-2218
    • Cazzolli, R.1    Carpenter, L.2    Biden, T.J.3    Schmitz-Peiffer, C.4
  • 62
    • 0038190982 scopus 로고    scopus 로고
    • Cdc42 is a Rho GTPase family member that can mediate insulin signaling to glucose transport in 3T3-L1 adipocytes
    • Usui I, Imamura T, Huang J, Satoh H, Olefsky JM 2003 Cdc42 is a Rho GTPase family member that can mediate insulin signaling to glucose transport in 3T3-L1 adipocytes. J Biol Chem 278:13765-13774
    • (2003) J Biol Chem , vol.278 , pp. 13765-13774
    • Usui, I.1    Imamura, T.2    Huang, J.3    Satoh, H.4    Olefsky, J.M.5
  • 63
    • 0037416217 scopus 로고    scopus 로고
    • Structure of Cdc42 in a complex with the GTPase-binding domain of the cell polarity protein, Par6
    • Garrard SM, Capaldo CT, Gao L, Rosen MK, Macara IG, Tomchick DR 2003 Structure of Cdc42 in a complex with the GTPase-binding domain of the cell polarity protein, Par6. EMBO J 22:1125-1133
    • (2003) EMBO J , vol.22 , pp. 1125-1133
    • Garrard, S.M.1    Capaldo, C.T.2    Gao, L.3    Rosen, M.K.4    Macara, I.G.5    Tomchick, D.R.6
  • 64
    • 0028338545 scopus 로고
    • Activation of phosphoinositide 3-kinase activity by Cdc42Hs binding to p85
    • Zheng Y, Bagrodia S, Cerione RA 1994 Activation of phosphoinositide 3-kinase activity by Cdc42Hs binding to p85. J Biol Chem 269:18727-18730
    • (1994) J Biol Chem , vol.269 , pp. 18727-18730
    • Zheng, Y.1    Bagrodia, S.2    Cerione, R.A.3
  • 65
    • 0029023942 scopus 로고
    • Rho family GTPases bind to phosphoinositide kinases
    • Tolias KF, Cantley LC, Carpenter CL 1995 Rho family GTPases bind to phosphoinositide kinases. J Biol Chem 270:17656-17659
    • (1995) J Biol Chem , vol.270 , pp. 17656-17659
    • Tolias, K.F.1    Cantley, L.C.2    Carpenter, C.L.3
  • 66
    • 0035846549 scopus 로고    scopus 로고
    • Akt mediates Rac/Cdc42-regulated cell motility in growth factor-stimulated cells and in invasive PTEN knockout cells
    • Higuchi M, Masuyama N, Fukui Y, Suzuki A, Gotoh Y 2001 Akt mediates Rac/Cdc42-regulated cell motility in growth factor-stimulated cells and in invasive PTEN knockout cells. Curr Biol 11:1958-1962
    • (2001) Curr Biol , vol.11 , pp. 1958-1962
    • Higuchi, M.1    Masuyama, N.2    Fukui, Y.3    Suzuki, A.4    Gotoh, Y.5
  • 67
    • 0034714352 scopus 로고    scopus 로고
    • Inhibition of insulin-induced glucose uptake by atypical protein kinase C isotype-specific interacting protein in 3T3-L1 adipocytes
    • Kotani K, Ogawa W, Hashiramoto M, Onishl T, Ohno S, Kasuga M 2000 Inhibition of insulin-induced glucose uptake by atypical protein kinase C isotype-specific interacting protein in 3T3-L1 adipocytes. J Biol Chem 275:26390-26395
    • (2000) J Biol Chem , vol.275 , pp. 26390-26395
    • Kotani, K.1    Ogawa, W.2    Hashiramoto, M.3    Onishl, T.4    Ohno, S.5    Kasuga, M.6
  • 68
    • 0032949091 scopus 로고    scopus 로고
    • PAR-6 is a conserved PDZ domain-containing protein that colocalizes with PAR-3 in Caenorhabditis elegans embryos
    • Hung TJ, Kemphues KJ 1999 PAR-6 is a conserved PDZ domain-containing protein that colocalizes with PAR-3 in Caenorhabditis elegans embryos. Development 126:127-135
    • (1999) Development , vol.126 , pp. 127-135
    • Hung, T.J.1    Kemphues, K.J.2
  • 69
    • 0000202186 scopus 로고    scopus 로고
    • A mammalian PAR-3-PAR-6 complex implicated in Cdc42/Rac1 and aPKC signalling and cell polarity
    • Lin D, Edwards AS, Fawcett JP, Mbamalu G, Scott JD, Pawson T 2000 A mammalian PAR-3-PAR-6 complex implicated in Cdc42/Rac1 and aPKC signalling and cell polarity. Nat Cell Biol 2:540-647
    • (2000) Nat Cell Biol , vol.2 , pp. 540-647
    • Lin, D.1    Edwards, A.S.2    Fawcett, J.P.3    Mbamalu, G.4    Scott, J.D.5    Pawson, T.6
  • 71
    • 0023392945 scopus 로고
    • High-efficiency transformation of mammalian cells by plasmid DNA
    • Chen C, Okayama H 1987 High-efficiency transformation of mammalian cells by plasmid DNA. Mol Cell Biol 7:2745-2752
    • (1987) Mol Cell Biol , vol.7 , pp. 2745-2752
    • Chen, C.1    Okayama, H.2
  • 72
    • 0032701466 scopus 로고    scopus 로고
    • Leptin stimulates glucose uptake in C2C12 muscle cells by activation of ERK2
    • Berti L, Gammeltoft S 1999 Leptin stimulates glucose uptake in C2C12 muscle cells by activation of ERK2. Mol Cell Endocrinol 157:121-130
    • (1999) Mol Cell Endocrinol , vol.157 , pp. 121-130
    • Berti, L.1    Gammeltoft, S.2
  • 73
    • 0037372045 scopus 로고    scopus 로고
    • Defective activation of atypical protein kinase C ζ and λ by insulin and phosphatidylinositol-3,4,5-(PO(4))(3) in skeletal muscle of rats following high-fat feeding and streptozotocin-induced diabetes
    • Kanoh Y, Sajan MP, Bandyopadhyay G, Miura A, Standaert ML, Farese RV 2003 Defective activation of atypical protein kinase C ζ and λ by insulin and phosphatidylinositol-3,4,5-(PO(4))(3) in skeletal muscle of rats following high-fat feeding and streptozotocin-induced diabetes. Endocrinology 144:947-954
    • (2003) Endocrinology , vol.144 , pp. 947-954
    • Kanoh, Y.1    Sajan, M.P.2    Bandyopadhyay, G.3    Miura, A.4    Standaert, M.L.5    Farese, R.V.6


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