메뉴 건너뛰기




Volumn 150, Issue 1, 2011, Pages 83-93

Regulation of IGF-1/PI3K/Akt signalling by the phosphoinositide phosphatase pharbin

Author keywords

Akt; IGF 1; Pharbin; PI3 kinase; protein synthesis

Indexed keywords

MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 3; PHARBIN; PHOSPHATASE; PHOSPHATIDYLINOSITOL 3 KINASE; PROTEIN KINASE B; PROTEIN SHIP2; PROTEIN SKIP; S6 KINASE; SOMATOMEDIN C; UNCLASSIFIED DRUG;

EID: 79960083029     PISSN: 0021924X     EISSN: 17562651     Source Type: Journal    
DOI: 10.1093/jb/mvr037     Document Type: Article
Times cited : (13)

References (40)
  • 2
    • 0036669037 scopus 로고    scopus 로고
    • Control of cell survival by IGF signaling pathways
    • DOI 10.1016/S1096-6374(02)00017-5
    • Vincent, A.M. and Feldman, E.L. (2002) Control of cell survival by IGF signaling pathways. Growth Horm. IGF Res. 12, 193-197 (Pubitemid 35230190)
    • (2002) Growth Hormone and IGF Research , vol.12 , Issue.4 , pp. 193-197
    • Vincent, A.M.1    Feldman, E.L.2
  • 3
    • 0037306190 scopus 로고    scopus 로고
    • Insulin/IGF and target of rapamycin signaling: A TOR de force in growth control
    • DOI 10.1016/S0962-8924(02)00042-9, PII S0962892402000429
    • Oldham, S. and Hafen, E. (2003) Insulin/IGF and target of rapamycin signaling: a TOR de force in growth control. Trends Cell Biol. 13, 79-85 (Pubitemid 36135889)
    • (2003) Trends in Cell Biology , vol.13 , Issue.2 , pp. 79-85
    • Oldham, S.1    Hafen, E.2
  • 4
    • 0037205048 scopus 로고    scopus 로고
    • The phosphoinositide 3-kinase pathway
    • DOI 10.1126/science.296.5573.1655
    • Cantley, L.C. (2002) The phosphoinositide 3-kinase pathway. Science. 296, 1655-1657 (Pubitemid 34579158)
    • (2002) Science , vol.296 , Issue.5573 , pp. 1655-1657
    • Cantley, L.C.1
  • 6
    • 13844312400 scopus 로고    scopus 로고
    • Phosphorylation and regulation of Akt/ PKB by the rictor-mTOR complex
    • Sarbassov, D.D., Guertin, D.A., Ali, S.M., and Sabatini, D.M. (2005) Phosphorylation and regulation of Akt/ PKB by the rictor-mTOR complex. Science 307, 1098-1101
    • (2005) Science , vol.307 , pp. 1098-1101
    • Sarbassov, D.D.1    Guertin, D.A.2    Ali, S.M.3    Sabatini, D.M.4
  • 7
    • 0024573591 scopus 로고
    • Insulin-like growth factor I stimulates elastin synthesis by bovine pulmonary arterial smooth muscle cells
    • DOI 10.1016/0006-291X(89)91667-7
    • Badesch, D.B., Lee, P.D., Parks, W.C., and Stenmark, K.R. (1989) Insulin-like growth factor I stimulates elastin synthesis by bovine pulmonary arterial smooth muscle cells. Biochem. Biophys. Res. Commun. 160, 382-387 (Pubitemid 19116508)
    • (1989) Biochemical and Biophysical Research Communications , vol.160 , Issue.1 , pp. 382-387
    • Badesch, D.B.1    Lee, P.D.K.2    Parks, W.C.3    Stenmark, K.R.4
  • 8
    • 0026518426 scopus 로고
    • Stimulation of cardiac protein synthesis by insulin-like growth factors
    • Fuller, S.J., Mynett, J.R., and Sugden, P.H. (1992) Stimulation of cardiac protein synthesis by insulin-like growth factors. Biochem. J. 282, 85-90
    • (1992) Biochem. J. , vol.282 , pp. 85-90
    • Fuller, S.J.1    Mynett, J.R.2    Sugden, P.H.3
  • 9
    • 0036295611 scopus 로고    scopus 로고
    • Regulation of cap-dependent translation by insulin-like growth factor-1 in neuronal cells
    • DOI 10.1006/bbrc.2002.6479
    • Quevedo, C., Salinas, M., and Alcazar, A. (2002) Regulation of cap-dependent translation by insulin-like growth factor-1 in neuronal cells. Biochem. Biophys. Res. Commun. 291, 560-566 (Pubitemid 34687381)
    • (2002) Biochemical and Biophysical Research Communications , vol.291 , Issue.3 , pp. 560-566
    • Quevedo, C.1    Salinas, M.2    Alcazar, A.3
  • 12
    • 0032834055 scopus 로고    scopus 로고
    • eIF4 initiation factors: Effectors of mRNA recruitment to ribosomes and regulators of translation
    • DOI 10.1146/annurev.biochem.68.1.913
    • Gingras, A.C., Raught, B., and Sonenberg, N. (1999) eIF4 initiation factors: effectors of mRNA recruitment to ribosomes and regulators of translation. Annu. Rev. Biochem. 68, 913-963 (Pubitemid 29449212)
    • (1999) Annual Review of Biochemistry , vol.68 , pp. 913-963
    • Gingras, A.-C.1    Raught, B.2    Sonenberg, N.3
  • 13
    • 0030832026 scopus 로고    scopus 로고
    • eIF4g dramatically enhances the binding of eIF4E to the mRNA 5'-cap structure
    • DOI 10.1074/jbc.272.35.21677
    • Haghighat, A. and Sonenberg, N. (1997) eIF4G dramatically enhances the binding of eIF4E to the mRNA 50-cap structure. J. Biol. Chem. 272, 21677-21680 (Pubitemid 27382778)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.35 , pp. 21677-21680
    • Haghighat, A.1    Sonenberg, N.2
  • 14
    • 0028034233 scopus 로고
    • Insulin-dependent stimulation of protein synthesis by phosphorylation of a regulator of 50-cap function
    • Pause, A., Belsham, G.J., Gingras, A.C., Donze, O., Lin, T.A., Lawrence, J.C. Jr, and Sonenberg, N. (1994) Insulin-dependent stimulation of protein synthesis by phosphorylation of a regulator of 50-cap function. Nature 371, 762-767
    • (1994) Nature , vol.371 , pp. 762-767
    • Pause, A.1    Belsham, G.J.2    Gingras, A.C.3    Donze, O.4    Lin, T.A.5    Lawrence Jr., J.C.6    Sonenberg, N.7
  • 16
    • 0030915898 scopus 로고    scopus 로고
    • Rapamycin suppresses 5'TOP mRNA translation through inhibition of p70(s6k)
    • DOI 10.1093/emboj/16.12.3693
    • Jefferies, H.B., Fumagalli, S., Dennis, P.B., Reinhard, C., Pearson, R.B., and Thomas, G. (1997) Rapamycin suppresses 50TOP mRNA translation through inhibition of p70s6k. EMBO J. 16, 3693-3704 (Pubitemid 27250062)
    • (1997) EMBO Journal , vol.16 , Issue.12 , pp. 3693-3704
    • Jefferies, H.B.J.1    Fumagalli, S.2    Dennis, P.B.3    Reinhard, C.4    Pearson, R.B.5    Thomas, G.6
  • 18
    • 77951568703 scopus 로고    scopus 로고
    • Phosphoinositide signalling in cancer: Beyond PI3K and PTEN
    • Bunney, T.D. and Katan, M. (2010) Phosphoinositide signalling in cancer: beyond PI3K and PTEN. Nat. Rev. Cancer 10, 342-352
    • (2010) Nat. Rev. Cancer , vol.10 , pp. 342-352
    • Bunney, T.D.1    Katan, M.2
  • 19
    • 34247139703 scopus 로고    scopus 로고
    • Regulation of class IA PI3Ks: Is there a role for monomeric PI3K subunits?
    • DOI 10.1042/BST0350199
    • Geering, B., Cutillas, P.R., and Vanhaesebroeck, B. (2007) Regulation of class IA PI3Ks: is there a role for monomeric PI3K subunits? Biochem. Soc. Trans. 35, 199-203 (Pubitemid 46596467)
    • (2007) Biochemical Society Transactions , vol.35 , Issue.2 , pp. 199-203
    • Geering, B.1    Cutillas, P.R.2    Vanhaesebroeck, B.3
  • 20
    • 34547114477 scopus 로고    scopus 로고
    • The inositol polyphosphate 5-phosphatases: Traffic controllers, waistline watchers and tumour suppressors?
    • Astle, M.V., Horan, K.A., Ooms, L.M., and Mitchell, C.A. (2007) The inositol polyphosphate 5-phosphatases: traffic controllers, waistline watchers and tumour suppressors? Biochem. Soc. Symp. 161-181
    • (2007) Biochem. Soc. Symp. , pp. 161-181
    • Astle, M.V.1    Horan, K.A.2    Ooms, L.M.3    Mitchell, C.A.4
  • 21
  • 23
    • 33746975370 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-phosphate [PtdIns(3)P] is generated at the plasma membrane by an inositol polyphosphate 5-phosphatase: Endogenous PtdIns(3)P can promote GLUT4 translocation to the plasma membrane
    • DOI 10.1128/MCB.00203-06
    • Kong, A.M., Horan, K.A., Sriratana, A., Bailey, C.G., Collyer, L.J., Nandurkar, H. H., Shisheva, A., Layton, M.J., Rasko, J.E., Rowe, T., and Mitchell, C.A. (2006) Phosphatidylinositol 3-phosphate [PtdIns3P] is generated at the plasma membrane by an inositol polyphosphate 5-phosphatase: endogenous PtdIns3P can promote GLUT4 translocation to the plasma membrane. Mol. Cell Biol. 26, 6065-6081 (Pubitemid 44204526)
    • (2006) Molecular and Cellular Biology , vol.26 , Issue.16 , pp. 6065-6081
    • Kong, A.M.1    Horan, K.A.2    Sriratana, A.3    Bailey, C.G.4    Collyer, L.J.5    Nandurkar, H.H.6    Shisheva, A.7    Layton, M.J.8    Rasko, J.E.J.9    Rowe, T.10    Mitchell, C.A.11
  • 27
    • 0032577699 scopus 로고    scopus 로고
    • The tumor suppressor, PTEN/MMAC1, dephosphorylates the lipid second messenger, phosphatidylinositol 3,4,5-trisphosphate
    • Maehama, T. and Dixon, J.E. (1998) The tumor suppressor, PTEN/MMAC1, dephosphorylates the lipid second messenger, phosphatidylinositol 3,4,5-trisphosphate. J. Biol. Chem. 273, 13375-13378
    • (1998) J. Biol. Chem. , vol.273 , pp. 13375-13378
    • Maehama, T.1    Dixon, J.E.2
  • 28
    • 0028802451 scopus 로고
    • The principal target of rapamycin-induced p70s6k inactivation is a novel phosphorylation site within a conserved hydrophobic domain
    • Pearson, R.B., Dennis, P.B., Han, J.W., Williamson, N.A., Kozma, S.C., Wettenhall, R.E., and Thomas, G. (1995) The principal target of rapamycin-induced p70s6k inactivation is a novel phosphorylation site within a conserved hydrophobic domain. EMBO J. 14, 5279-5287
    • (1995) EMBO J. , vol.14 , pp. 5279-5287
    • Pearson, R.B.1    Dennis, P.B.2    Han, J.W.3    Williamson, N.A.4    Kozma, S.C.5    Wettenhall, R.E.6    Thomas, G.7
  • 29
    • 0032511022 scopus 로고    scopus 로고
    • Phosphorylation sites in the autoinhibitory domain participate in p70(s6k) activation loop phosphorylation
    • DOI 10.1074/jbc.273.24.14845
    • Dennis, P.B., Pullen, N., Pearson, R.B., Kozma, S.C., and Thomas, G. (1998) Phosphorylation sites in the autoinhibitory domain participate in p70(s6k) activation loop phosphorylation. J. Biol. Chem. 273, 14845-14852 (Pubitemid 28272772)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.24 , pp. 14845-14852
    • Dennis, P.B.1    Pullen, N.2    Pearson, R.B.3    Kozma, S.C.4    Thomas, G.5
  • 32
    • 0035869175 scopus 로고    scopus 로고
    • PTEN inhibits insulin-stimulated MEK/MAPK activation and cell growth by blocking IRS-1 phosphorylation and IRS-1/Grb-2/Sos complex formation in a breast cancer model
    • Weng, L.P., Smith, W.M., Brown, J.L., and Eng, C. (2001) PTEN inhibits insulin-stimulated MEK/MAPK activation and cell growth by blocking IRS-1 phosphorylation and IRS-1/Grb-2/Sos complex formation in a breast cancer model. Hum. Mol. Genet. 10, 605-616 (Pubitemid 32229365)
    • (2001) Human Molecular Genetics , vol.10 , Issue.6 , pp. 605-616
    • Weng, L.-P.1    Smith, W.M.2    Brown, J.L.3    Eng, C.4
  • 33
    • 0042421683 scopus 로고    scopus 로고
    • Dual role of Src homology domain 2-containing inositol phosphatase 2 in the regulation of platelet-derived growth factor and insulin-like growth factor I signaling in rat vascular smooth muscle cells
    • DOI 10.1210/en.2003-0190
    • Sasaoka, T., Kikuchi, K., Wada, T., Sato, A., Hori, H., Murakami, S., Fukui, K., Ishihara, H., Aota, R., Kimura, I., and Kobayashi, M. (2003) Dual role of SRC homology domain 2-containing inositol phosphatase 2 in the regulation of platelet-derived growth factor and insulin-like growth factor I signaling in rat vascular smooth muscle cells. Endocrinol. 144, 4204-4214 (Pubitemid 37088777)
    • (2003) Endocrinology , vol.144 , Issue.9 , pp. 4204-4214
    • Sasaoka, T.1    Kikuchi, K.2    Wada, T.3    Sato, A.4    Hori, H.5    Murakami, S.6    Fukui, K.7    Ishihara, H.8    Aota, R.9    Kimura, I.10    Kobayashi, M.11
  • 34
    • 23944456384 scopus 로고    scopus 로고
    • Skeletal muscle hypertrophy and atrophy signaling pathways
    • DOI 10.1016/j.biocel.2005.04.018, PII S1357272505001317
    • Glass, D.J. (2005) Skeletal muscle hypertrophy and atrophy signaling pathways. Int. J. Biochem. Cell Biol. 37, 1974-1984 (Pubitemid 41206815)
    • (2005) International Journal of Biochemistry and Cell Biology , vol.37 , Issue.10 SPEC. ISS. , pp. 1974-1984
    • Glass, D.J.1
  • 35
    • 0034724747 scopus 로고    scopus 로고
    • The tumor suppressor PTEN negatively regulates insulin signaling in 3T3- L1 adipocytes
    • DOI 10.1074/jbc.275.17.12889
    • Nakashima, N., Sharma, P.M., Imamura, T., Bookstein, R., and Olefsky, J.M. (2000) The tumor suppressor PTEN negatively regulates insulin signaling in 3T3-L1 adipocytes. J. Biol. Chem. 275, 12889-12895 (Pubitemid 30241444)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.17 , pp. 12889-12895
    • Nakashima, N.1    Sharma, P.M.2    Imamura, T.3    Bookstein, R.4    Olefsky, J.M.5
  • 36
    • 0037312905 scopus 로고    scopus 로고
    • SKIP negatively regulates insulin-induced GLUT4 translocation and membrane ruffle formation
    • DOI 10.1128/MCB.23.4.1209-1220.2003
    • Ijuin, T. and Takenawa, T. (2003) SKIP negatively regulates insulin-induced GLUT4 translocation and membrane ruffle formation. Mol. Cell Biol. 23, 1209-1220 (Pubitemid 36177031)
    • (2003) Molecular and Cellular Biology , vol.23 , Issue.4 , pp. 1209-1220
    • Ijuin, T.1    Takenawa, T.2
  • 37
    • 0032583205 scopus 로고    scopus 로고
    • Matrix-dependent Tiam1/Rac signaling in epithelial cells promotes either cell-cell adhesion or cell migration and is regulated by phosphatidylinositol 3-kinase
    • DOI 10.1083/jcb.143.5.1385
    • Sander, E.E, van Delft, S., ten Klooster, J.P., Reid, T., van der Kammen, R.A., Michiels, F., and Collard, J.G. (1998) Matrix-dependent Tiam1/Rac signaling in epithelial cells promotes either cell-cell adhesion or cell migration and is regulated by phosphatidylinositol 3-kinase. J. Cell Biol. 143, 1385-1398 (Pubitemid 28559838)
    • (1998) Journal of Cell Biology , vol.143 , Issue.5 , pp. 1385-1398
    • Sander, E.E.1    Van Delft, S.2    Ten Klooster, J.P.3    Reid, T.4    Van Der Kammen, R.A.5    Michiels, F.6    Collard, J.G.7
  • 38
    • 15144353776 scopus 로고    scopus 로고
    • Role of substrates and products of PI 3-kinase in regulating activation of Rac-related guanosine triphosphatases by Vav
    • Han, J., Luby-Phelps, K., Das, B., Shu, X., Xia, Y., Mosteller, R.D., Krishna, U.M., Falck, J.R., White, M.A., and Broek, D. (1998) Role of substrates and products of PI 3-kinase in regulating activation of Rac-related guanosine triphosphatases by Vav. Science 279, 558-560
    • (1998) Science , vol.279 , pp. 558-560
    • Han, J.1    Luby-Phelps, K.2    Das, B.3    Shu, X.4    Xia, Y.5    Mosteller, R.D.6    Krishna, U.M.7    Falck, J.R.8    White, M.A.9    Broek, D.10
  • 40
    • 27144529532 scopus 로고    scopus 로고
    • PDGFRαα signaling is regulated through the primary cilium in fibroblasts
    • DOI 10.1016/j.cub.2005.09.012, PII S0960982205010365
    • Schneider, L., Clement, C.A., Teilmann, S.C., Pazour, G.J., Hoffmann, E.K., Satir, P., and Christensen, S.T. (2005) PDGFRalphaalpha signaling is regulated through the primary cilium in fibroblasts. Curr. Biol. 15, 1861-1866 (Pubitemid 41501522)
    • (2005) Current Biology , vol.15 , Issue.20 , pp. 1861-1866
    • Schneider, L.1    Clement, C.A.2    Teilmann, S.C.3    Pazour, G.J.4    Hoffmann, E.K.5    Satir, P.6    Christensen, S.T.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.