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Volumn 73, Issue 18, 2013, Pages 5742-5753

Akt SUM Oylation regulates cell proliferation and tumorigenesis

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; ARGININE; GLUTAMIC ACID; LYSINE; PROTEIN INHIBITOR OF ACTIVATED STAT; PROTEIN KINASE B; PROTEIN SENP1; PROTEIN UBC9; SUMO 1 PROTEIN; SUMO PROTEIN; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG; MESSENGER RNA; SMALL INTERFERING RNA; UBIQUITIN CONJUGATING ENZYME; UBIQUITIN CONJUGATING ENZYME UBC9; UBIQUITIN-CONJUGATING ENZYME UBC9;

EID: 84884761456     PISSN: 00085472     EISSN: 15387445     Source Type: Journal    
DOI: 10.1158/0008-5472.CAN-13-0538     Document Type: Article
Times cited : (124)

References (43)
  • 1
  • 2
    • 84864222562 scopus 로고    scopus 로고
    • Atypical ubiquitylation - The unexplored world of polyubiquitin beyond Lys48 and Lys63 linkages
    • Kulathu Y, Komander D. Atypical ubiquitylation - the unexplored world of polyubiquitin beyond Lys48 and Lys63 linkages. Nat Rev Mol Cell Biol 2012;13:508-23.
    • (2012) Nat Rev Mol Cell Biol , vol.13 , pp. 508-523
    • Kulathu, Y.1    Komander, D.2
  • 3
    • 49349107518 scopus 로고    scopus 로고
    • Lysine acetylation: Codified crosstalk with other posttranslational modifications
    • Yang XJ, Seto E. Lysine acetylation: codified crosstalk with other posttranslational modifications. Mol Cell 2008;31:449-61.
    • (2008) Mol Cell , vol.31 , pp. 449-461
    • Yang, X.J.1    Seto, E.2
  • 4
    • 78649396592 scopus 로고    scopus 로고
    • The SUMOpathway: Emerging mechanisms that shape specificity, conjugation and recognition
    • Gareau JR, Lima CD. The SUMOpathway: emerging mechanisms that shape specificity, conjugation and recognition. Nat Rev Mol Cell Biol 2010;11:861-71.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 861-871
    • Gareau, J.R.1    Lima, C.D.2
  • 5
    • 3943099375 scopus 로고    scopus 로고
    • Protein modification by SUMO
    • Johnson ES. Protein modification by SUMO. Annu Rev Biochem 2004;73:355-82.
    • (2004) Annu Rev Biochem , vol.73 , pp. 355-382
    • Johnson, E.S.1
  • 6
    • 36349022018 scopus 로고    scopus 로고
    • Emerging extranuclear roles of protein SUMOylation in neuronal function and dysfunction
    • Martin S, Wilkinson KA, Nishimune A, Henley JM. Emerging extranuclear roles of protein SUMOylation in neuronal function and dysfunction. Nat Rev Neurosci 2007;8:948-59.
    • (2007) Nat Rev Neurosci , vol.8 , pp. 948-959
    • Martin, S.1    Wilkinson, K.A.2    Nishimune, A.3    Henley, J.M.4
  • 7
    • 44649163272 scopus 로고    scopus 로고
    • The type i TGF-beta receptor is covalently modified and regulated by sumoylation
    • Kang JS, Saunier EF, Akhurst RJ, Derynck R. The type I TGF-beta receptor is covalently modified and regulated by sumoylation. Nat Cell Biol 2008;10:654-64.
    • (2008) Nat Cell Biol , vol.10 , pp. 654-664
    • Kang, J.S.1    Saunier, E.F.2    Akhurst, R.J.3    Derynck, R.4
  • 8
    • 79952280325 scopus 로고    scopus 로고
    • Oncogenic Ras abrogates MEK SUMOylation that suppresses the ERK pathway and cell transformation
    • Kubota Y, O'Grady P, Saito H, Takekawa M. Oncogenic Ras abrogates MEK SUMOylation that suppresses the ERK pathway and cell transformation. Nat Cell Biol 2011;13:282-91.
    • (2011) Nat Cell Biol , vol.13 , pp. 282-291
    • Kubota, Y.1    O'grady, P.2    Saito, H.3    Takekawa, M.4
  • 9
    • 40949145324 scopus 로고    scopus 로고
    • Extracellular signal-regulated kinase 5 SUMOylation antagonizes shear stress-induced antiinflammatory response and endothelial nitric oxide synthase expression in endothelial cells
    • Woo CH, Shishido T, McClain C, Lim JH, Li JD, Yang J, et al. Extracellular signal-regulated kinase 5 SUMOylation antagonizes shear stress-induced antiinflammatory response and endothelial nitric oxide synthase expression in endothelial cells. Circ Res 2008;102:538-45.
    • (2008) Circ Res , vol.102 , pp. 538-545
    • Woo, C.H.1    Shishido, T.2    McClain, C.3    Lim, J.H.4    Li, J.D.5    Yang, J.6
  • 13
    • 34250788809 scopus 로고    scopus 로고
    • AKT/PKB signaling: Navigating downstream
    • Manning BD, Cantley LC. AKT/PKB signaling: navigating downstream. Cell 2007;129:1261-74.
    • (2007) Cell , vol.129 , pp. 1261-1274
    • Manning, B.D.1    Cantley, L.C.2
  • 14
    • 77951917753 scopus 로고    scopus 로고
    • Regulation of Akt signaling activation by ubiquitination
    • Yang WL, Wu CY, Wu J, Lin HK. Regulation of Akt signaling activation by ubiquitination. Cell Cycle 2010;9:487-97.
    • (2010) Cell Cycle , vol.9 , pp. 487-497
    • Yang, W.L.1    Wu, C.Y.2    Wu, J.3    Lin, H.K.4
  • 15
  • 16
    • 84861552793 scopus 로고    scopus 로고
    • The Skp2-SCF E3 ligase regulates Akt ubiquitination, glycolysis, herceptin sensitivity, and tumorigenesis
    • Chan CH, Li CF, Yang WL, Gao Y, Lee SW, Feng Z, et al. The Skp2-SCF E3 ligase regulates Akt ubiquitination, glycolysis, herceptin sensitivity, and tumorigenesis. Cell 2012;149:1098-111.
    • (2012) Cell , vol.149 , pp. 1098-1111
    • Chan, C.H.1    Li, C.F.2    Yang, W.L.3    Gao, Y.4    Lee, S.W.5    Feng, Z.6
  • 17
  • 18
    • 84872736566 scopus 로고    scopus 로고
    • Ubiquitin-dependent regulation of phospho-AKT dynamics by the ubiquitin E3 ligase, NEDD4-1, in the insulin-like growth factor-1 response
    • Fan CD, Lum MA, Xu C, Black JD, Wang X. Ubiquitin-dependent regulation of phospho-AKT dynamics by the ubiquitin E3 ligase, NEDD4-1, in the insulin-like growth factor-1 response. J Biol Chem 2013;288:1674-84.
    • (2013) J Biol Chem , vol.288 , pp. 1674-1684
    • Fan, C.D.1    Lum, M.A.2    Xu, C.3    Black, J.D.4    Wang, X.5
  • 19
    • 0038404927 scopus 로고    scopus 로고
    • Inhibition of heat shock protein 90 function down-regulates Akt kinase and sensitizes tumors to Taxol
    • Solit DB, Basso AD, Olshen AB, Scher HI, Rosen N. Inhibition of heat shock protein 90 function down-regulates Akt kinase and sensitizes tumors to Taxol. Cancer Res 2003;63:2139-44.
    • (2003) Cancer Res , vol.63 , pp. 2139-2144
    • Solit, D.B.1    Basso, A.D.2    Olshen, A.B.3    Scher, H.I.4    Rosen, N.5
  • 20
    • 79960620082 scopus 로고    scopus 로고
    • The deacetylase SIRT1 promotes membrane localization and activation of Akt and PDK1 during tumorigenesis and cardiac hypertrophy
    • Sundaresan NR, Pillai VB, Wolfgeher D, Samant S, Vasudevan P, Parekh V, et al. The deacetylase SIRT1 promotes membrane localization and activation of Akt and PDK1 during tumorigenesis and cardiac hypertrophy. Sci Signal 2011;4:ra46.
    • (2011) Sci Signal , vol.4
    • Sundaresan, N.R.1    Pillai, V.B.2    Wolfgeher, D.3    Samant, S.4    Vasudevan, P.5    Parekh, V.6
  • 21
    • 77953310667 scopus 로고    scopus 로고
    • The Fbw7/human CDC4 tumor suppressor targets proproliferative factor KLF5 for ubiquitination and degradation through multiple phosphodegron motifs
    • Liu N, Li H, Li S, Shen M, Xiao N, Chen Y, et al. The Fbw7/human CDC4 tumor suppressor targets proproliferative factor KLF5 for ubiquitination and degradation through multiple phosphodegron motifs. J Biol Chem 2010;285:18858-67.
    • (2010) J Biol Chem , vol.285 , pp. 18858-18867
    • Liu, N.1    Li, H.2    Li, S.3    Shen, M.4    Xiao, N.5    Chen, Y.6
  • 22
    • 84862907678 scopus 로고    scopus 로고
    • Ubiquitin-specific protease 4 (USP4) targets TRAF2 and TRAF6 for deubiquitination and inhibits TNFalpha-induced cancer cell migration
    • Xiao N, Li H, Luo J, Wang R, Chen H, Chen J, et al. Ubiquitin-specific protease 4 (USP4) targets TRAF2 and TRAF6 for deubiquitination and inhibits TNFalpha-induced cancer cell migration. Biochem J 2012;441: 979-86.
    • (2012) Biochem J , vol.441 , pp. 979-986
    • Xiao, N.1    Li, H.2    Luo, J.3    Wang, R.4    Chen, H.5    Chen, J.6
  • 23
    • 74949127215 scopus 로고    scopus 로고
    • Detection of proteins sumoylated in vivo and in vitro
    • Sarge KD, Park-Sarge OK. Detection of proteins sumoylated in vivo and in vitro. Methods Mol Biol 2009;590:265-77.
    • (2009) Methods Mol Biol , vol.590 , pp. 265-277
    • Sarge, K.D.1    Park-Sarge, O.K.2
  • 24
    • 13244273504 scopus 로고    scopus 로고
    • Asubcellular prefractionation protocol for minute amounts of mammalian cell cultures and tissue
    • Guillemin I, Becker M, Ociepka K, Friauf E, Nothwang HG. Asubcellular prefractionation protocol for minute amounts of mammalian cell cultures and tissue. Proteomics 2005;5:35-45.
    • (2005) Proteomics , vol.5 , pp. 35-45
    • Guillemin, I.1    Becker, M.2    Ociepka, K.3    Friauf, E.4    Nothwang, H.G.5
  • 25
    • 84878728282 scopus 로고    scopus 로고
    • FBW7regulates endothelial functions by targeting KLF2 for ubiquitination and degradation
    • Wang R, Wang Y, Liu N, Ren C, Jiang C, Zhang K, et al.FBW7regulates endothelial functions by targeting KLF2 for ubiquitination and degradation. Cell Res 2013;23:803-19.
    • (2013) Cell Res , vol.23 , pp. 803-819
    • Wang, R.1    Wang, Y.2    Liu, N.3    Ren, C.4    Jiang, C.5    Zhang, K.6
  • 26
    • 0029079275 scopus 로고
    • The protein kinase encoded by the Akt proto-oncogene is a target of the PDGF-activated phosphatidylinositol 3-kinase
    • Franke TF, Yang SI, Chan TO, Datta K, Kazlauskas A, Morrison DK, et al. The protein kinase encoded by the Akt proto-oncogene is a target of the PDGF-activated phosphatidylinositol 3-kinase. Cell 1995;81: 727-36.
    • (1995) Cell , vol.81 , pp. 727-736
    • Franke, T.F.1    Yang, S.I.2    Chan, T.O.3    Datta, K.4    Kazlauskas, A.5    Morrison, D.K.6
  • 27
    • 84872413578 scopus 로고    scopus 로고
    • SUMO: A multifaceted modifier of chromatin structure and function
    • Cubenas-Potts C, Matunis MJ. SUMO: a multifaceted modifier of chromatin structure and function. Dev Cell 2013;24:1-12.
    • (2013) Dev Cell , vol.24 , pp. 1-12
    • Cubenas-Potts, C.1    Matunis, M.J.2
  • 28
    • 33847649960 scopus 로고    scopus 로고
    • Ubc9 fusion-directed SUMOylation (UFDS): A method to analyze function of protein SUMOylation
    • Jakobs A, Koehnke J, Himstedt F, Funk M, Korn B, Gaestel M, et al. Ubc9 fusion-directed SUMOylation (UFDS): a method to analyze function of protein SUMOylation. Nat Methods 2007;4:245-50.
    • (2007) Nat Methods , vol.4 , pp. 245-250
    • Jakobs, A.1    Koehnke, J.2    Himstedt, F.3    Funk, M.4    Korn, B.5    Gaestel, M.6
  • 29
    • 79952189085 scopus 로고    scopus 로고
    • SUMOylation promotes de novo targeting of HP1alpha to pericentric heterochromatin
    • Maison C, Bailly D, Roche D, Montes de Oca R, Probst AV, Vassias I, et al. SUMOylation promotes de novo targeting of HP1alpha to pericentric heterochromatin. Nat Genet 2011;43:220-7.
    • (2011) Nat Genet , vol.43 , pp. 220-227
    • Maison, C.1    Bailly, D.2    Roche, D.3    Montes De Oca, R.4    Probst, A.V.5    Vassias, I.6
  • 30
    • 34347222583 scopus 로고    scopus 로고
    • Design and implementation of bimolecular fluorescence complementation (BiFC) assays for the visualization of protein interactions in living cells
    • Kerppola TK. Design and implementation of bimolecular fluorescence complementation (BiFC) assays for the visualization of protein interactions in living cells. Nat Protoc 2006;1:1278-86.
    • (2006) Nat Protoc , vol.1 , pp. 1278-1286
    • Kerppola, T.K.1
  • 31
    • 32644459132 scopus 로고    scopus 로고
    • Regulation of cytokine signaling pathways by PIAS proteins
    • Shuai K. Regulation of cytokine signaling pathways by PIAS proteins. Cell Res 2006;16:196-202.
    • (2006) Cell Res , vol.16 , pp. 196-202
    • Shuai, K.1
  • 32
    • 23444461182 scopus 로고    scopus 로고
    • Regulation of gene-activation pathways by PIAS proteins in the immune system
    • Shuai K, Liu B. Regulation of gene-activation pathways by PIAS proteins in the immune system. Nat Rev Immunol 2005;5:593-605.
    • (2005) Nat Rev Immunol , vol.5 , pp. 593-605
    • Shuai, K.1    Liu, B.2
  • 33
    • 47949125486 scopus 로고    scopus 로고
    • The mammalian target of rapamycin complex 2 controls folding and stability of Akt and protein kinase C
    • Facchinetti V, Ouyang W, Wei H, Soto N, Lazorchak A, Gould C, et al. The mammalian target of rapamycin complex 2 controls folding and stability of Akt and protein kinase C. EMBO J 2008;27:1932-43.
    • (2008) EMBO J , vol.27 , pp. 1932-1943
    • Facchinetti, V.1    Ouyang, W.2    Wei, H.3    Soto, N.4    Lazorchak, A.5    Gould, C.6
  • 34
    • 0028912932 scopus 로고
    • AH/ PH domain-mediated interaction between Akt molecules and its potential role in Akt regulation
    • Datta K, Franke TF, Chan TO, Makris A, Yang SI, Kaplan DR, et al. AH/ PH domain-mediated interaction between Akt molecules and its potential role in Akt regulation. Mol Cell Biol 1995;15:2304-10.
    • (1995) Mol Cell Biol , vol.15 , pp. 2304-2310
    • Datta, K.1    Franke, T.F.2    Chan, T.O.3    Makris, A.4    Yang, S.I.5    Kaplan, D.R.6
  • 36
    • 0034643331 scopus 로고    scopus 로고
    • AFX-like Forkhead transcription factors mediate cell-cycle regulation by Ras and PKB through p27kip1
    • Medema RH, Kops GJ, Bos JL, Burgering BM. AFX-like Forkhead transcription factors mediate cell-cycle regulation by Ras and PKB through p27kip1. Nature 2000;404:782-7.
    • (2000) Nature , vol.404 , pp. 782-787
    • Medema, R.H.1    Kops, G.J.2    Bos, J.L.3    Burgering, B.M.4
  • 38
    • 84871443133 scopus 로고    scopus 로고
    • Heterologous SUMO-2/3-ubiquitin chains optimize IkBa degradation and NF-kB activity
    • Aillet F, Lopitz-Otsoa F, Egana I, Hjerpe R, Fraser P, Hay RT, et al. Heterologous SUMO-2/3-ubiquitin chains optimize IkBa degradation and NF-kB activity. PLoS One 2012;7:e51672.
    • (2012) PLoS One , vol.7
    • Aillet, F.1    Lopitz-Otsoa, F.2    Egana, I.3    Hjerpe, R.4    Fraser, P.5    Hay, R.T.6
  • 40
    • 84874372046 scopus 로고    scopus 로고
    • Genomic analysis of non-NF2 meningiomas reveals mutations in TRAF7, KLF4, AKT1, and SMO
    • Clark VE, Erson-Omay EZ, Serin A, Yin J, Cotney J, Ozduman K, et al. Genomic analysis of non-NF2 meningiomas reveals mutations in TRAF7, KLF4, AKT1, and SMO. Science 2013;339:1077-80.
    • (2013) Science , vol.339 , pp. 1077-1080
    • Clark, V.E.1    Erson-Omay, E.Z.2    Serin, A.3    Yin, J.4    Cotney, J.5    Ozduman, K.6
  • 41
    • 84874771475 scopus 로고    scopus 로고
    • Profiling of ubiquitin-like modifications reveals features of mitotic control
    • Merbl Y, Refour P, Patel H, Springer M, Kirschner MW. Profiling of ubiquitin-like modifications reveals features of mitotic control. Cell 2013;152:1160-72.
    • (2013) Cell , vol.152 , pp. 1160-1172
    • Merbl, Y.1    Refour, P.2    Patel, H.3    Springer, M.4    Kirschner, M.W.5
  • 43
    • 84863336040 scopus 로고    scopus 로고
    • SUMO1 modification of PTEN regulates tumorigenesis by controlling its association with the plasma membrane
    • Huang J, Yan J, Zhang J, Zhu S, Wang Y, Shi T, et al. SUMO1 modification of PTEN regulates tumorigenesis by controlling its association with the plasma membrane. Nat Commun 2012;3:911.
    • (2012) Nat Commun , vol.3 , pp. 911
    • Huang, J.1    Yan, J.2    Zhang, J.3    Zhu, S.4    Wang, Y.5    Shi, T.6


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