메뉴 건너뛰기




Volumn 30, Issue 2, 2016, Pages 290-307

Regulation of OGT by URI in Response to Glucose Confers c-MYC-Dependent Survival Mechanisms

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; CYCLIC AMP; CYCLIC AMP DEPENDENT PROTEIN KINASE; GLUCOSE; MYC PROTEIN; O LINKED N ACETYLGLUCOSAMINE TRANSFERASE; PHOSPHOPROTEIN PHOSPHATASE 1; PHOSPHOPROTEIN PHOSPHATASE 1 GAMMA; TRANSFERASE; UNCLASSIFIED DRUG; UNCONVENTIONAL PREFOLDIN RPB5 INTERACTOR; MYC PROTEIN, HUMAN; MYC PROTEIN, MOUSE; N ACETYLGLUCOSAMINYLTRANSFERASE; SIGNAL PEPTIDE; SMALL INTERFERING RNA; URI1 PROTEIN, HUMAN;

EID: 84989968256     PISSN: 15356108     EISSN: 18783686     Source Type: Journal    
DOI: 10.1016/j.ccell.2016.06.023     Document Type: Article
Times cited : (75)

References (39)
  • 1
    • 33746907024 scopus 로고    scopus 로고
    • Subcellular dynamics of protein kinase A activity visualized by FRET-based reporters
    • Allen, M.D., Zhang, J., Subcellular dynamics of protein kinase A activity visualized by FRET-based reporters. Biochem. Biophys. Res. Commun. 348 (2006), 716–721.
    • (2006) Biochem. Biophys. Res. Commun. , vol.348 , pp. 716-721
    • Allen, M.D.1    Zhang, J.2
  • 2
    • 33751217466 scopus 로고    scopus 로고
    • Tumor morphology and phenotypic evolution driven by selective pressure from the microenvironment
    • Anderson, A.R., Weaver, A.M., Cummings, P.T., Quaranta, V., Tumor morphology and phenotypic evolution driven by selective pressure from the microenvironment. Cell 127 (2006), 905–915.
    • (2006) Cell , vol.127 , pp. 905-915
    • Anderson, A.R.1    Weaver, A.M.2    Cummings, P.T.3    Quaranta, V.4
  • 3
    • 77955279255 scopus 로고    scopus 로고
    • The extended PP1 toolkit: designed to create specificity
    • Bollen, M., Peti, W., Ragusa, M.J., Beullens, M., The extended PP1 toolkit: designed to create specificity. Trends Biochem. Sci. 35 (2010), 450–458.
    • (2010) Trends Biochem. Sci. , vol.35 , pp. 450-458
    • Bollen, M.1    Peti, W.2    Ragusa, M.J.3    Beullens, M.4
  • 4
    • 77952429792 scopus 로고    scopus 로고
    • Nutrient sensor O-GlcNAc transferase regulates breast cancer tumorigenesis through targeting of the oncogenic transcription factor FoxM1
    • Caldwell, S.A., Jackson, S.R., Shahriari, K.S., Lynch, T.P., Sethi, G., Walker, S., Vosseller, K., Reginato, M.J., Nutrient sensor O-GlcNAc transferase regulates breast cancer tumorigenesis through targeting of the oncogenic transcription factor FoxM1. Oncogene 29 (2010), 2831–2842.
    • (2010) Oncogene , vol.29 , pp. 2831-2842
    • Caldwell, S.A.1    Jackson, S.R.2    Shahriari, K.S.3    Lynch, T.P.4    Sethi, G.5    Walker, S.6    Vosseller, K.7    Reginato, M.J.8
  • 5
    • 84881056831 scopus 로고    scopus 로고
    • MYC, metabolism, cell growth, and tumorigenesis
    • Dang, C.V., MYC, metabolism, cell growth, and tumorigenesis. Cold Spring Harb. Perspect. Med., 3, 2013, 10.1101/cshperspect.a014217.
    • (2013) Cold Spring Harb. Perspect. Med. , vol.3
    • Dang, C.V.1
  • 8
    • 34948823880 scopus 로고    scopus 로고
    • S6K1-mediated disassembly of mitochondrial URI/PP1gamma complexes activates a negative feedback program that counters S6K1 survival signaling
    • Djouder, N., Metzler, S.C., Schmidt, A., Wirbelauer, C., Gstaiger, M., Aebersold, R., Hess, D., Krek, W., S6K1-mediated disassembly of mitochondrial URI/PP1gamma complexes activates a negative feedback program that counters S6K1 survival signaling. Mol. Cell 28 (2007), 28–40.
    • (2007) Mol. Cell , vol.28 , pp. 28-40
    • Djouder, N.1    Metzler, S.C.2    Schmidt, A.3    Wirbelauer, C.4    Gstaiger, M.5    Aebersold, R.6    Hess, D.7    Krek, W.8
  • 9
    • 27144528715 scopus 로고    scopus 로고
    • Inhibition of mitochondrial respiration elevates oxygen concentration but leaves regulation of hypoxia-inducible factor (HIF) intact
    • Doege, K., Heine, S., Jensen, I., Jelkmann, W., Metzen, E., Inhibition of mitochondrial respiration elevates oxygen concentration but leaves regulation of hypoxia-inducible factor (HIF) intact. Blood 106 (2005), 2311–2317.
    • (2005) Blood , vol.106 , pp. 2311-2317
    • Doege, K.1    Heine, S.2    Jensen, I.3    Jelkmann, W.4    Metzen, E.5
  • 11
    • 34248216634 scopus 로고    scopus 로고
    • An evolutionary hybrid cellular automaton model of solid tumour growth
    • Gerlee, P., Anderson, A.R., An evolutionary hybrid cellular automaton model of solid tumour growth. J. Theor. Biol. 246 (2007), 583–603.
    • (2007) J. Theor. Biol. , vol.246 , pp. 583-603
    • Gerlee, P.1    Anderson, A.R.2
  • 12
    • 77954627336 scopus 로고    scopus 로고
    • Diffusion-limited tumour growth: simulations and analysis
    • Gerlee, P., Anderson, A.R., Diffusion-limited tumour growth: simulations and analysis. Math. Biosci. Eng. 7 (2010), 385–400.
    • (2010) Math. Biosci. Eng. , vol.7 , pp. 385-400
    • Gerlee, P.1    Anderson, A.R.2
  • 13
    • 18144395012 scopus 로고    scopus 로고
    • Importance of a surface hydrophobic pocket on protein phosphatase-1 catalytic subunit in recognizing cellular regulators
    • Gibbons, J.A., Weiser, D.C., Shenolikar, S., Importance of a surface hydrophobic pocket on protein phosphatase-1 catalytic subunit in recognizing cellular regulators. J. Biol. Chem. 280 (2005), 15903–15911.
    • (2005) J. Biol. Chem. , vol.280 , pp. 15903-15911
    • Gibbons, J.A.1    Weiser, D.C.2    Shenolikar, S.3
  • 15
    • 2142790225 scopus 로고    scopus 로고
    • O-linked N-acetylglucosamine levels in cerebellar neurons respond reciprocally to pertubations of phosphorylation
    • Griffith, L.S., Schmitz, B., O-linked N-acetylglucosamine levels in cerebellar neurons respond reciprocally to pertubations of phosphorylation. Eur. J. Biochem. 262 (1999), 824–831.
    • (1999) Eur. J. Biochem. , vol.262 , pp. 824-831
    • Griffith, L.S.1    Schmitz, B.2
  • 16
    • 84905723395 scopus 로고    scopus 로고
    • Nutrient regulation of signaling, transcription, and cell physiology by O-GlcNAcylation
    • Hardiville, S., Hart, G.W., Nutrient regulation of signaling, transcription, and cell physiology by O-GlcNAcylation. Cell Metab. 20 (2014), 208–213.
    • (2014) Cell Metab. , vol.20 , pp. 208-213
    • Hardiville, S.1    Hart, G.W.2
  • 17
    • 67649874094 scopus 로고    scopus 로고
    • The O-GlcNAc modification
    • A. Varki R.D. Cummings J.D. Esko H.H. Freeze P. Stanley C.R. Bertozzi G.W. Hart M.E. Etzler Cold Spring Harbor Laboratory Press Cold Spring Harbor, NY Chapter 18
    • Hart, G.W., Akimoto, Y., The O-GlcNAc modification. Varki, A., Cummings, R.D., Esko, J.D., Freeze, H.H., Stanley, P., Bertozzi, C.R., Hart, G.W., Etzler, M.E., (eds.) Essentials of Glycobiology, 2009, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY Chapter 18.
    • (2009) Essentials of Glycobiology
    • Hart, G.W.1    Akimoto, Y.2
  • 18
    • 0037166352 scopus 로고    scopus 로고
    • Dynamic interplay between O-glycosylation and O-phosphorylation of nucleocytoplasmic proteins: alternative glycosylation/phosphorylation of THR-58, a known mutational hot spot of c-Myc in lymphomas, is regulated by mitogens
    • Kamemura, K., Hayes, B.K., Comer, F.I., Hart, G.W., Dynamic interplay between O-glycosylation and O-phosphorylation of nucleocytoplasmic proteins: alternative glycosylation/phosphorylation of THR-58, a known mutational hot spot of c-Myc in lymphomas, is regulated by mitogens. J. Biol. Chem. 277 (2002), 19229–19235.
    • (2002) J. Biol. Chem. , vol.277 , pp. 19229-19235
    • Kamemura, K.1    Hayes, B.K.2    Comer, F.I.3    Hart, G.W.4
  • 20
    • 79251611901 scopus 로고    scopus 로고
    • Structure of human O-GlcNAc transferase and its complex with a peptide substrate
    • Lazarus, M.B., Nam, Y., Jiang, J., Sliz, P., Walker, S., Structure of human O-GlcNAc transferase and its complex with a peptide substrate. Nature 469 (2011), 564–567.
    • (2011) Nature , vol.469 , pp. 564-567
    • Lazarus, M.B.1    Nam, Y.2    Jiang, J.3    Sliz, P.4    Walker, S.5
  • 21
    • 0037442984 scopus 로고    scopus 로고
    • Mitochondrial and nucleocytoplasmic targeting of O-linked GlcNAc transferase
    • Love, D.C., Kochan, J., Cathey, R.L., Shin, S.H., Hanover, J.A., Mitochondrial and nucleocytoplasmic targeting of O-linked GlcNAc transferase. J. Cell Sci. 116 (2003), 647–654.
    • (2003) J. Cell Sci. , vol.116 , pp. 647-654
    • Love, D.C.1    Kochan, J.2    Cathey, R.L.3    Shin, S.H.4    Hanover, J.A.5
  • 22
    • 84918523488 scopus 로고    scopus 로고
    • Cancer metabolism and elevated O-GlcNAc in oncogenic signaling
    • Ma, Z., Vosseller, K., Cancer metabolism and elevated O-GlcNAc in oncogenic signaling. J. Biol. Chem. 289 (2014), 34457–34465.
    • (2014) J. Biol. Chem. , vol.289 , pp. 34457-34465
    • Ma, Z.1    Vosseller, K.2
  • 24
    • 78650324886 scopus 로고    scopus 로고
    • Downregulation of c-MYC protein levels contributes to cancer cell survival under dual deficiency of oxygen and glucose
    • Okuyama, H., Endo, H., Akashika, T., Kato, K., Inoue, M., Downregulation of c-MYC protein levels contributes to cancer cell survival under dual deficiency of oxygen and glucose. Cancer Res. 70 (2010), 10213–10223.
    • (2010) Cancer Res. , vol.70 , pp. 10213-10223
    • Okuyama, H.1    Endo, H.2    Akashika, T.3    Kato, K.4    Inoue, M.5
  • 28
    • 0032539534 scopus 로고    scopus 로고
    • A unique glucose-dependent apoptotic pathway induced by c-Myc
    • Shim, H., Chun, Y.S., Lewis, B.C., Dang, C.V., A unique glucose-dependent apoptotic pathway induced by c-Myc. Proc. Natl. Acad. Sci. USA 95 (1998), 1511–1516.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 1511-1516
    • Shim, H.1    Chun, Y.S.2    Lewis, B.C.3    Dang, C.V.4
  • 29
    • 77956396629 scopus 로고    scopus 로고
    • O-GlcNAc signaling: a metabolic link between diabetes and cancer?
    • Slawson, C., Copeland, R.J., Hart, G.W., O-GlcNAc signaling: a metabolic link between diabetes and cancer?. Trends Biochem. Sci. 35 (2010), 547–555.
    • (2010) Trends Biochem. Sci. , vol.35 , pp. 547-555
    • Slawson, C.1    Copeland, R.J.2    Hart, G.W.3
  • 30
    • 75849131117 scopus 로고    scopus 로고
    • The ups and downs of Myc biology
    • Soucek, L., Evan, G.I., The ups and downs of Myc biology. Curr. Opin. Genet. Dev. 20 (2010), 91–95.
    • (2010) Curr. Opin. Genet. Dev. , vol.20 , pp. 91-95
    • Soucek, L.1    Evan, G.I.2
  • 31
    • 40949111343 scopus 로고    scopus 로고
    • GLUT1 and GLUT9 as major contributors to glucose influx in HepG2 cells identified by a high sensitivity intramolecular FRET glucose sensor
    • Takanaga, H., Chaudhuri, B., Frommer, W.B., GLUT1 and GLUT9 as major contributors to glucose influx in HepG2 cells identified by a high sensitivity intramolecular FRET glucose sensor. Biochim. Biophys. Acta 1778 (2008), 1091–1099.
    • (2008) Biochim. Biophys. Acta , vol.1778 , pp. 1091-1099
    • Takanaga, H.1    Chaudhuri, B.2    Frommer, W.B.3
  • 34
    • 4644262462 scopus 로고    scopus 로고
    • O-GlcNAc transferase is in a functional complex with protein phosphatase 1 catalytic subunits
    • Wells, L., Kreppel, L.K., Comer, F.I., Wadzinski, B.E., Hart, G.W., O-GlcNAc transferase is in a functional complex with protein phosphatase 1 catalytic subunits. J. Biol. Chem. 279 (2004), 38466–38470.
    • (2004) J. Biol. Chem. , vol.279 , pp. 38466-38470
    • Wells, L.1    Kreppel, L.K.2    Comer, F.I.3    Wadzinski, B.E.4    Hart, G.W.5
  • 35
    • 0000904661 scopus 로고
    • Localization of the primary metabolic block produced by 2-deoxyglucose
    • Wick, A.N., Drury, D.R., Nakada, H.I., Wolfe, J.B., Localization of the primary metabolic block produced by 2-deoxyglucose. J. Biol. Chem. 224 (1957), 963–969.
    • (1957) J. Biol. Chem. , vol.224 , pp. 963-969
    • Wick, A.N.1    Drury, D.R.2    Nakada, H.I.3    Wolfe, J.B.4
  • 38
    • 84864766367 scopus 로고    scopus 로고
    • O-GlcNAcylation plays a role in tumor recurrence of hepatocellular carcinoma following liver transplantation
    • Zhu, Q., Zhou, L., Yang, Z., Lai, M., Xie, H., Wu, L., Xing, C., Zhang, F., Zheng, S., O-GlcNAcylation plays a role in tumor recurrence of hepatocellular carcinoma following liver transplantation. Med. Oncol. 29 (2012), 985–993.
    • (2012) Med. Oncol. , vol.29 , pp. 985-993
    • Zhu, Q.1    Zhou, L.2    Yang, Z.3    Lai, M.4    Xie, H.5    Wu, L.6    Xing, C.7    Zhang, F.8    Zheng, S.9
  • 39
    • 84988527756 scopus 로고    scopus 로고
    • O-GlcNAcylation of histone deacetylases 1 in hepatocellular carcinoma promotes cancer progression
    • Zhu, G., Tao, T., Zhang, D., Liu, X., Qiu, H., Han, L., Xu, Z., Xiao, Y., Cheng, C., Shen, A., O-GlcNAcylation of histone deacetylases 1 in hepatocellular carcinoma promotes cancer progression. Glycobiology, 2016, 1–14, 10.1093/glycob/cww025.
    • (2016) Glycobiology , pp. 1-14
    • Zhu, G.1    Tao, T.2    Zhang, D.3    Liu, X.4    Qiu, H.5    Han, L.6    Xu, Z.7    Xiao, Y.8    Cheng, C.9    Shen, A.10


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.