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Volumn 407, Issue 2, 2007, Pages 231-241

Regulation of multisite phosphorylation and 14-3-3 binding of AS160 in response to IGF-1, EGF, PMA and AICAR

Author keywords

14 3 3; Akt substrate of 160 kDa (AS160); Akt protein kinase B (PKB); GTPase activating protein (GAP); p90 ribosomal S6 kinase (RSK); Serum and glucocorticoid induced protein kinase (SGK)

Indexed keywords

AKT SUBSTRATE OF 160 KDA (AS160); AKT/PROTEIN KINASE B (PKB); GTPASE-ACTIVATING PROTEIN (GAP); P90 RIBOSOMAL S6 KINASE (RSK); SERUM- AND GLUCOCORTICOID-INDUCED PROTEIN KINASE (SGK);

EID: 35048903018     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20070649     Document Type: Article
Times cited : (151)

References (49)
  • 1
    • 3242788127 scopus 로고    scopus 로고
    • Dynamic interactions between 14-3-3 proteins and phosphoproteins regulate diverse cellular processes
    • MacKintosh, C. (2004) Dynamic interactions between 14-3-3 proteins and phosphoproteins regulate diverse cellular processes. Biochem. J. 381, 329-342
    • (2004) Biochem. J , vol.381 , pp. 329-342
    • MacKintosh, C.1
  • 2
    • 21044434194 scopus 로고    scopus 로고
    • Targeted proteomic analysis of 14-3-3σ, a p53 effector commonly silenced in cancer
    • Benzinger, A., Muster, N., Koch, H. B., Yates, 3rd, J. R. and Hermeking, H. (2005) Targeted proteomic analysis of 14-3-3σ, a p53 effector commonly silenced in cancer. Mol. Cell. Proteomics 4, 785-795
    • (2005) Mol. Cell. Proteomics , vol.4 , pp. 785-795
    • Benzinger, A.1    Muster, N.2    Koch, H.B.3    Yates 3rd, J.R.4    Hermeking, H.5
  • 3
    • 4344598183 scopus 로고    scopus 로고
    • Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization
    • Jin, J., Smith, F. D., Stark, C., Wells, C. D., Fawcett, J. P., Kulkarni, S., Metalnikov, P., O'Donnell, P., Taylor, P., Taylor, L. et al. (2004) Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization. Curr. Biol. 14, 1436-1450
    • (2004) Curr. Biol , vol.14 , pp. 1436-1450
    • Jin, J.1    Smith, F.D.2    Stark, C.3    Wells, C.D.4    Fawcett, J.P.5    Kulkarni, S.6    Metalnikov, P.7    O'Donnell, P.8    Taylor, P.9    Taylor, L.10
  • 4
    • 3543035767 scopus 로고    scopus 로고
    • Comprehensive proteomic analysis of interphase and mitotic 14-3-3-binding proteins
    • Meek, S. E., Lane, W. S. and Piwnica-Worms, H. (2004) Comprehensive proteomic analysis of interphase and mitotic 14-3-3-binding proteins. J. Biol. Chem. 279, 32046-32054
    • (2004) J. Biol. Chem , vol.279 , pp. 32046-32054
    • Meek, S.E.1    Lane, W.S.2    Piwnica-Worms, H.3
  • 5
    • 2342651419 scopus 로고    scopus 로고
    • 14-3-3-affinity purification of over 200 human phosphoproteins reveals new links to regulation of cellular metabolism, proliferation and trafficking
    • Pozuelo Rubio, M., Geraghty, K. M., Wong, B. H., Wood, N. T., Campbell, D. G., Morrice, N. and Mackintosh, C. (2004) 14-3-3-affinity purification of over 200 human phosphoproteins reveals new links to regulation of cellular metabolism, proliferation and trafficking. Biochem. J. 379, 395-408
    • (2004) Biochem. J , vol.379 , pp. 395-408
    • Pozuelo Rubio, M.1    Geraghty, K.M.2    Wong, B.H.3    Wood, N.T.4    Campbell, D.G.5    Morrice, N.6    Mackintosh, C.7
  • 6
    • 0036905341 scopus 로고    scopus 로고
    • Regulation of the 14-3-3-binding protein p39 by growth factors and nutrients in rat PC12 pheochromocytoma cells
    • Harthill, J. E., Pozuelo Rubio, M., Milne, F. C. and MacKintosh, C. (2002) Regulation of the 14-3-3-binding protein p39 by growth factors and nutrients in rat PC12 pheochromocytoma cells. Biochem. J. 368, 565-572
    • (2002) Biochem. J , vol.368 , pp. 565-572
    • Harthill, J.E.1    Pozuelo Rubio, M.2    Milne, F.C.3    MacKintosh, C.4
  • 7
    • 0041312686 scopus 로고    scopus 로고
    • 14-3-3s regulate fructose-2,6-bisphosphate levels by binding to PKB-phosphorylated cardiac fructose-2,6-bisphosphate kinase/phosphatase
    • Pozuelo Rubio, M., Peggie, M., Wong, B. H., Morrice, N. and MacKintosh, C. (2003) 14-3-3s regulate fructose-2,6-bisphosphate levels by binding to PKB-phosphorylated cardiac fructose-2,6-bisphosphate kinase/phosphatase. EMBO J. 22, 3514-3523
    • (2003) EMBO J , vol.22 , pp. 3514-3523
    • Pozuelo Rubio, M.1    Peggie, M.2    Wong, B.H.3    Morrice, N.4    MacKintosh, C.5
  • 9
    • 0037160104 scopus 로고    scopus 로고
    • Regulation of TSC2 by 14-3-3 binding
    • Li, Y., Inoki, K., Yeung, R. and Guan, K. L. (2002) Regulation of TSC2 by 14-3-3 binding. J. Biol. Chem. 277, 44593-44596
    • (2002) J. Biol. Chem , vol.277 , pp. 44593-44596
    • Li, Y.1    Inoki, K.2    Yeung, R.3    Guan, K.L.4
  • 11
    • 0035868368 scopus 로고    scopus 로고
    • Roles of the forkhead in rhabdomyosarcoma (FKHR) phosphorylation sites in regulating 14-3-3 binding, transactivation and nuclear targetting
    • Rena, G., Prescott, A. R., Guo, S., Cohen, P. and Unterman, T. G. (2001) Roles of the forkhead in rhabdomyosarcoma (FKHR) phosphorylation sites in regulating 14-3-3 binding, transactivation and nuclear targetting. Biochem. J. 354, 605-612
    • (2001) Biochem. J , vol.354 , pp. 605-612
    • Rena, G.1    Prescott, A.R.2    Guo, S.3    Cohen, P.4    Unterman, T.G.5
  • 12
    • 34249738710 scopus 로고    scopus 로고
    • Resistance exercise and insulin regulate AS160 and interaction with 14-3-3 in human skeletal muscle
    • Howlett, K. F., Sakamoto, K., Garnham, A., Cameron-Smith, D. and Hargreaves, M. (2007) Resistance exercise and insulin regulate AS160 and interaction with 14-3-3 in human skeletal muscle. Diabetes 56, 1608-1614
    • (2007) Diabetes , vol.56 , pp. 1608-1614
    • Howlett, K.F.1    Sakamoto, K.2    Garnham, A.3    Cameron-Smith, D.4    Hargreaves, M.5
  • 13
    • 33749395733 scopus 로고    scopus 로고
    • A role for 14-3-3 in insulin-stimulated GLUT4 translocation through its interaction with the RabGAP AS160
    • Ramm, G., Larance, M., Guilhaus, M. and James, D. E. (2006) A role for 14-3-3 in insulin-stimulated GLUT4 translocation through its interaction with the RabGAP AS160. J. Biol. Chem. 281, 29174-29180
    • (2006) J. Biol. Chem , vol.281 , pp. 29174-29180
    • Ramm, G.1    Larance, M.2    Guilhaus, M.3    James, D.E.4
  • 14
    • 0037151026 scopus 로고    scopus 로고
    • A method to identify serine kinase substrates. Akt phosphorylates a novel adipocyte protein with a Rab GTPase-activating protein (GAP) domain
    • Kane, S., Sano, H., Liu, S. C., Asara, J. M., Lane, W. S., Garner, C. C. and Lienhard, G. E. (2002) A method to identify serine kinase substrates. Akt phosphorylates a novel adipocyte protein with a Rab GTPase-activating protein (GAP) domain. J. Biol. Chem. 277, 22115-22118
    • (2002) J. Biol. Chem , vol.277 , pp. 22115-22118
    • Kane, S.1    Sano, H.2    Liu, S.C.3    Asara, J.M.4    Lane, W.S.5    Garner, C.C.6    Lienhard, G.E.7
  • 15
    • 0346250165 scopus 로고    scopus 로고
    • Cellular mechanism of insulin resistance: Potential links with inflammation
    • Perseghin, G., Petersen, K. and Shulman, G. I. (2003) Cellular mechanism of insulin resistance: potential links with inflammation Int. J. Obes. Relat. Metab. Disord. 27 (Suppl. 3), S6-S11
    • (2003) Int. J. Obes. Relat. Metab. Disord , vol.27 , Issue.SUPPL. 3
    • Perseghin, G.1    Petersen, K.2    Shulman, G.I.3
  • 16
    • 33846178185 scopus 로고    scopus 로고
    • Rabs 8A and 14 are targets of the insulin-regulated Rab-GAP AS160 regulating GLUT4 traffic in muscle cells
    • Ishikura, S., Bilan, P. J. and Klip, A. (2007) Rabs 8A and 14 are targets of the insulin-regulated Rab-GAP AS160 regulating GLUT4 traffic in muscle cells. Biochem. Biophys. Res. Commun. 353, 1074-1079
    • (2007) Biochem. Biophys. Res. Commun , vol.353 , pp. 1074-1079
    • Ishikura, S.1    Bilan, P.J.2    Klip, A.3
  • 18
    • 26844573782 scopus 로고    scopus 로고
    • AS160, the Akt substrate regulating GLUT4 translocation, has a functional Rab GTPase-activating protein domain
    • Miinea, C. P., Sano, H., Kane, S., Sano, E., Fukuda, M., Peranen, J., Lane, W. S. and Lienhard, G. E. (2005) AS160, the Akt substrate regulating GLUT4 translocation, has a functional Rab GTPase-activating protein domain. Biochem. J. 391, 87-93
    • (2005) Biochem. J , vol.391 , pp. 87-93
    • Miinea, C.P.1    Sano, H.2    Kane, S.3    Sano, E.4    Fukuda, M.5    Peranen, J.6    Lane, W.S.7    Lienhard, G.E.8
  • 19
    • 33947578085 scopus 로고    scopus 로고
    • Rab10, a target of the AS160 Rab GAP, is reguired for insulin-stimulated translocation of GLUT4 to the adipocyte plasma membrane
    • Sano, H., Eguez, L., Teruel, M. N., Fukuda, M., Chuang, T. D., Chavez, J. A., Lienhard, G. E. and McGraw, T. E. (2007) Rab10, a target of the AS160 Rab GAP, is reguired for insulin-stimulated translocation of GLUT4 to the adipocyte plasma membrane. Cell Metab. 5, 293-303
    • (2007) Cell Metab , vol.5 , pp. 293-303
    • Sano, H.1    Eguez, L.2    Teruel, M.N.3    Fukuda, M.4    Chuang, T.D.5    Chavez, J.A.6    Lienhard, G.E.7    McGraw, T.E.8
  • 20
    • 20044389885 scopus 로고    scopus 로고
    • Insulin-stimulated phosphorylation of the Akt substrate AS160 is impaired in skeletal muscle of type 2 diabetic subjects
    • Karlsson, H. K., Zierath, J. R., Kane, S., Krook, A., Lienhard, G. E. and Wallberg-Henriksson, H. (2005) Insulin-stimulated phosphorylation of the Akt substrate AS160 is impaired in skeletal muscle of type 2 diabetic subjects. Diabetes 54, 1692-1697
    • (2005) Diabetes , vol.54 , pp. 1692-1697
    • Karlsson, H.K.1    Zierath, J.R.2    Kane, S.3    Krook, A.4    Lienhard, G.E.5    Wallberg-Henriksson, H.6
  • 21
    • 33645997012 scopus 로고    scopus 로고
    • Bridging the GAP between insulin signaling and GLUT4 translocation
    • Watson, R. T. and Pessin, J. E. (2006) Bridging the GAP between insulin signaling and GLUT4 translocation. Trends Biochem. Sci. 31, 215-222
    • (2006) Trends Biochem. Sci , vol.31 , pp. 215-222
    • Watson, R.T.1    Pessin, J.E.2
  • 22
    • 0037677096 scopus 로고    scopus 로고
    • Insulin-stimulated phosphorylation of a Rab GTPase-activating protein regulates GLUT4 translocation
    • Sano, H., Kane, S., Sano, E., Miinea, C. P., Asara, J. M., Lane, W. S., Garner, C. W. and Lienhard, G. E. (2003) Insulin-stimulated phosphorylation of a Rab GTPase-activating protein regulates GLUT4 translocation. J. Biol. Chem. 278, 14599-14602
    • (2003) J. Biol. Chem , vol.278 , pp. 14599-14602
    • Sano, H.1    Kane, S.2    Sano, E.3    Miinea, C.P.4    Asara, J.M.5    Lane, W.S.6    Garner, C.W.7    Lienhard, G.E.8
  • 23
    • 33749365543 scopus 로고    scopus 로고
    • Interaction of the Akt substrate, AS160, with the glucose transporter 4 vesicle marker protein, insulin-regulated aminopeptidase
    • Peck, G. R., Ye, S., Pham, V., Fernando, R. N., Macaulay, S. L., Chai, S. Y. and Albiston, A. L. (2006) Interaction of the Akt substrate, AS160, with the glucose transporter 4 vesicle marker protein, insulin-regulated aminopeptidase. Mol. Endocrinol. 20, 2576-2583
    • (2006) Mol. Endocrinol , vol.20 , pp. 2576-2583
    • Peck, G.R.1    Ye, S.2    Pham, V.3    Fernando, R.N.4    Macaulay, S.L.5    Chai, S.Y.6    Albiston, A.L.7
  • 28
    • 33847062845 scopus 로고    scopus 로고
    • The Rab GTPase-activating protein AS160 integrates Akt, protein kinase C, and AMP-activated protein kinase signals regulating GLUT4 traffic
    • Thong, F. S., Bilan, P. J. and Klip, A. (2007) The Rab GTPase-activating protein AS160 integrates Akt, protein kinase C, and AMP-activated protein kinase signals regulating GLUT4 traffic. Diabetes 56, 414-423
    • (2007) Diabetes , vol.56 , pp. 414-423
    • Thong, F.S.1    Bilan, P.J.2    Klip, A.3
  • 29
    • 12144271277 scopus 로고    scopus 로고
    • Increased phosphorylation of Akt substrate of 160 kDa (AS160) in rat skeletal muscle in response to insulin or contractile activity
    • Bruss, M. D., Arias, E. B., Lienhard, G. E. and Cartee, G. D. (2005) Increased phosphorylation of Akt substrate of 160 kDa (AS160) in rat skeletal muscle in response to insulin or contractile activity. Diabetes 54, 41-50
    • (2005) Diabetes , vol.54 , pp. 41-50
    • Bruss, M.D.1    Arias, E.B.2    Lienhard, G.E.3    Cartee, G.D.4
  • 31
    • 0037178786 scopus 로고    scopus 로고
    • mTOR interacts with raptor to form a nutrient-sensitive complex that signals to the cell growth machinery
    • Kim, D. H., Sarbassov, D. D., Ali, S. M., King, J. E., Latek, R. R., Erdjument-Bromage, H., Tempst, P. and Sabatini, D. M. (2002) mTOR interacts with raptor to form a nutrient-sensitive complex that signals to the cell growth machinery. Cell 110, 163-175
    • (2002) Cell , vol.110 , pp. 163-175
    • Kim, D.H.1    Sarbassov, D.D.2    Ali, S.M.3    King, J.E.4    Latek, R.R.5    Erdjument-Bromage, H.6    Tempst, P.7    Sabatini, D.M.8
  • 33
    • 33644674733 scopus 로고    scopus 로고
    • Automated identification and quantification of protein phosphorylation sites by LC/MS on a hybrid triple quadrupole linear ion trap mass spectrometer
    • Williamson, B. L., Marchese, J. and Morrice, N. A. (2006) Automated identification and quantification of protein phosphorylation sites by LC/MS on a hybrid triple quadrupole linear ion trap mass spectrometer. Mol. Cell. Proteomics 5, 337-346
    • (2006) Mol. Cell. Proteomics , vol.5 , pp. 337-346
    • Williamson, B.L.1    Marchese, J.2    Morrice, N.A.3
  • 35
    • 0030603158 scopus 로고    scopus 로고
    • Inhibition of protein kinase Cμ by various inhibitors. Differentiation from protein kinase c isoenzymes
    • Gschwendt, M., Dieterich, S., Rennecke, J., Kittstein, W., Mueller, H. J. and Johannes, F. J. (1996) Inhibition of protein kinase Cμ by various inhibitors. Differentiation from protein kinase c isoenzymes. FEBS Lett. 392, 77-80
    • (1996) FEBS Lett , vol.392 , pp. 77-80
    • Gschwendt, M.1    Dieterich, S.2    Rennecke, J.3    Kittstein, W.4    Mueller, H.J.5    Johannes, F.J.6
  • 36
    • 0037507252 scopus 로고    scopus 로고
    • The mammalian target of rapamycin (mTOR) partner, raptor, binds the mTOR substrates p70 S6 kinase and 4E-BP1 through their TOR signaling (TOS) motif
    • Nojima, H., Tokunaga, C., Eguchi, S., Oshiro, N., Hidayat, S., Yoshino, K., Hara, K., Tanaka, N., Avruch, J. and Yonezawa, K. (2003) The mammalian target of rapamycin (mTOR) partner, raptor, binds the mTOR substrates p70 S6 kinase and 4E-BP1 through their TOR signaling (TOS) motif. J. Biol. Chem. 278, 15461-15464
    • (2003) J. Biol. Chem , vol.278 , pp. 15461-15464
    • Nojima, H.1    Tokunaga, C.2    Eguchi, S.3    Oshiro, N.4    Hidayat, S.5    Yoshino, K.6    Hara, K.7    Tanaka, N.8    Avruch, J.9    Yonezawa, K.10
  • 37
    • 0037205409 scopus 로고    scopus 로고
    • Regulation of an activated S6 kinase 1 variant reveals a novel mammalian target of rapamycin phosphorylation site
    • Saitoh, M., Pullen, N., Brennan, P., Cantrell, D., Dennis, P. B. and Thomas, G. (2002) Regulation of an activated S6 kinase 1 variant reveals a novel mammalian target of rapamycin phosphorylation site. J. Biol. Chem. 277, 20104-20112
    • (2002) J. Biol. Chem , vol.277 , pp. 20104-20112
    • Saitoh, M.1    Pullen, N.2    Brennan, P.3    Cantrell, D.4    Dennis, P.B.5    Thomas, G.6
  • 38
    • 0037117409 scopus 로고    scopus 로고
    • Identification of a conserved motif required for mTOR signaling
    • Schalm, S. S. and Blenis, J. (2002) Identification of a conserved motif required for mTOR signaling. Curr. Biol. 12, 632-639
    • (2002) Curr. Biol , vol.12 , pp. 632-639
    • Schalm, S.S.1    Blenis, J.2
  • 39
    • 33745225026 scopus 로고    scopus 로고
    • AMP-activated protein kinase: Development of the energy sensor concept
    • Hardie, D. G., Hawley, S. A. and Scott, J. W. (2006) AMP-activated protein kinase: development of the energy sensor concept. J. Physiol. 574, 7-15
    • (2006) J. Physiol , vol.574 , pp. 7-15
    • Hardie, D.G.1    Hawley, S.A.2    Scott, J.W.3
  • 41
    • 32544456122 scopus 로고    scopus 로고
    • α2 Isoform-specific activation of 5′adenosine monophosphate-activated protein kinase by 5-aminoimidazole-4-carboxamide-1-β-D-ribonucleoside at a physiological level activates glucose transport and increases glucose transporter 4 in mouse skeletal muscle
    • Nakano, M., Hamada, T., Hayashi, T., Yonemitsu, S., Miyamoto, L., Toyoda, T., Tanaka, S., Masuzaki, H., Ebihara, K., Ogawa, Y. et al. (2006) α2 Isoform-specific activation of 5′adenosine monophosphate-activated protein kinase by 5-aminoimidazole-4-carboxamide-1-β-D-ribonucleoside at a physiological level activates glucose transport and increases glucose transporter 4 in mouse skeletal muscle. Metabolism 55, 300-308
    • (2006) Metabolism , vol.55 , pp. 300-308
    • Nakano, M.1    Hamada, T.2    Hayashi, T.3    Yonemitsu, S.4    Miyamoto, L.5    Toyoda, T.6    Tanaka, S.7    Masuzaki, H.8    Ebihara, K.9    Ogawa, Y.10
  • 42
    • 20944436591 scopus 로고    scopus 로고
    • Effects of metformin and rosiglitazone treatment on insulin signaling and glucose uptake in patients with newly diagnosed type 2 diabetes: A randomized controlled study
    • Karlsson, H. K., Hallsten, K., Bjornholm, M., Tsuchida, H., Chibalin, A. V., Virtanen, K. A., Heinonen, O. J., Lonnqvist, F., Nuutila, P. and Zierath, J. R. (2005) Effects of metformin and rosiglitazone treatment on insulin signaling and glucose uptake in patients with newly diagnosed type 2 diabetes: a randomized controlled study. Diabetes 54, 1459-1467
    • (2005) Diabetes , vol.54 , pp. 1459-1467
    • Karlsson, H.K.1    Hallsten, K.2    Bjornholm, M.3    Tsuchida, H.4    Chibalin, A.V.5    Virtanen, K.A.6    Heinonen, O.J.7    Lonnqvist, F.8    Nuutila, P.9    Zierath, J.R.10
  • 43
    • 0035881737 scopus 로고    scopus 로고
    • A novel method to identify protein kinase substrates: EEF2 kinase is phosphorylated and inhibited by SAPK4/p38δ
    • Knebel, A., Morrice, N. and Cohen, P. (2001) A novel method to identify protein kinase substrates: eEF2 kinase is phosphorylated and inhibited by SAPK4/p38δ. EMBO J. 20, 4360-4369
    • (2001) EMBO J , vol.20 , pp. 4360-4369
    • Knebel, A.1    Morrice, N.2    Cohen, P.3
  • 45
    • 3042818799 scopus 로고    scopus 로고
    • Regulation of the TSC pathway by LKB1: Evidence of a molecular link between tuberous sclerosis complex and Peutz-Jeghers syndrome
    • Corradetti, M. N., Inoki, K., Bardeesy, N., DePinho, R. A. and Guan, K. L. (2004) Regulation of the TSC pathway by LKB1: evidence of a molecular link between tuberous sclerosis complex and Peutz-Jeghers syndrome. Genes Dev. 18, 1533-1538
    • (2004) Genes Dev , vol.18 , pp. 1533-1538
    • Corradetti, M.N.1    Inoki, K.2    Bardeesy, N.3    DePinho, R.A.4    Guan, K.L.5
  • 46
    • 0345167800 scopus 로고    scopus 로고
    • TSC2 mediates cellular energy response to control cell growth and survival
    • Inoki, K., Zhu, T. and Guan, K. L. (2003) TSC2 mediates cellular energy response to control cell growth and survival. Cell 115, 577-590
    • (2003) Cell , vol.115 , pp. 577-590
    • Inoki, K.1    Zhu, T.2    Guan, K.L.3
  • 49
    • 34247148430 scopus 로고    scopus 로고
    • Substrate specificity and effect on GLUT4 translocation of the Rab GTPase-activating protein TBC1D1
    • Roach, W. G., Chavez, J. A., Miinea, C. P. and Lienhard, G. E. (2007) Substrate specificity and effect on GLUT4 translocation of the Rab GTPase-activating protein TBC1D1. Biochem. J. 403, 353-358
    • (2007) Biochem. J , vol.403 , pp. 353-358
    • Roach, W.G.1    Chavez, J.A.2    Miinea, C.P.3    Lienhard, G.E.4


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