메뉴 건너뛰기




Volumn 12, Issue 12, 2013, Pages 3489-3497

Regulation of protein degradation by O-GlcNAcylation: Crosstalk with ubiquitination

Author keywords

[No Author keywords available]

Indexed keywords

CAMP RESPONSE ELEMENT BINDING PROTEIN TRANSCRIPTION COACTIVATOR 2; CASEIN KINASE II; CASEIN KINASE II ALPHA; COP9 SIGNALOSOME; CRYPTOCHROME 1; CRYPTOCHROME 2; CYCLIC AMP BINDING PROTEIN; CYTOKERATIN 18; CYTOKERATIN 8; ESTROGEN RECEPTOR BETA; FORSKOLIN; HISTONE; LACTOFERRIN; N ACETYLGLUCOSAMINE; PER1 PROTEIN; PER2 PROTEIN; PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR GAMMA COACTIVATOR 1ALPHA; PROTEASOME; PROTEASOME INHIBITOR; PROTEIN; PROTEIN P53; TRANSCRIPTION FACTOR CLOCK; TRANSCRIPTION FACTOR SNAIL; TRANSCRIPTION FACTOR SNAIL1; UBIQUITIN; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG; UNINDEXED DRUG; UVOMORULIN; ZINC FINGER PROTEIN; ZINC FINGER PROTEIN A20;

EID: 84890731711     PISSN: 15359476     EISSN: 15359484     Source Type: Journal    
DOI: 10.1074/mcp.R113.029751     Document Type: Review
Times cited : (141)

References (97)
  • 1
    • 2442437350 scopus 로고
    • Isolation of a polypeptide that has lymphocytedifferentiating properties and is probably represented universally in living cells
    • Goldstein, G., Scheid, M., Hammerling, U., Schlesinger, D. H., Niall, H. D., and Boyse, E. A. (1975) Isolation of a polypeptide that has lymphocytedifferentiating properties and is probably represented universally in living cells. Proc. Natl. Acad. Sci. U.S.A. 72, 11-15
    • (1975) Proc. Natl. Acad. Sci. U.S.A. , vol.72 , pp. 11-15
    • Goldstein, G.1    Scheid, M.2    Hammerling, U.3    Schlesinger, D.H.4    Niall, H.D.5    Boyse, E.A.6
  • 2
    • 77953715170 scopus 로고    scopus 로고
    • Regulatory mechanisms involved in the control of ubiquitin homeostasis
    • Kimura, Y., and Tanaka, K. (2010) Regulatory mechanisms involved in the control of ubiquitin homeostasis. J Biochem. 147, 793-798
    • (2010) J Biochem. , vol.147 , pp. 793-798
    • Kimura, Y.1    Tanaka, K.2
  • 4
    • 44649101850 scopus 로고    scopus 로고
    • Atypical ubiquitin chains: New molecular signals
    • Ikeda, F., and Dikic, I. (2008) Atypical ubiquitin chains: new molecular signals. EMBO Rep. 9, 536-542
    • (2008) EMBO Rep. , vol.9 , pp. 536-542
    • Ikeda, F.1    Dikic, I.2
  • 5
    • 0035293622 scopus 로고    scopus 로고
    • Protein regulation by monoubiquitin
    • Hicke, L. (2001) Protein regulation by monoubiquitin. Nat. Rev. Mol. Cell Biol. 2, 195-201
    • (2001) Nat. Rev. Mol. Cell Biol. , vol.2 , pp. 195-201
    • Hicke, L.1
  • 6
    • 36749010218 scopus 로고    scopus 로고
    • The age of crosstalk: Phosphorylation, ubiquitination, and beyond
    • Hunter, T. (2007) The age of crosstalk: phosphorylation, ubiquitination, and beyond. Mol. Cell 28, 730-738
    • (2007) Mol. Cell , vol.28 , pp. 730-738
    • Hunter, T.1
  • 7
    • 24044547036 scopus 로고    scopus 로고
    • Regulating the regulators: Control of protein ubiquitination and ubiquitin-like modifications by extracellular stimuli
    • Gao, M., and Karin, M. (2005) Regulating the regulators: control of protein ubiquitination and ubiquitin-like modifications by extracellular stimuli. Mol. Cell 19, 581-593
    • (2005) Mol. Cell , vol.19 , pp. 581-593
    • Gao, M.1    Karin, M.2
  • 8
    • 17844385784 scopus 로고    scopus 로고
    • Regulatory cross-talk between lysine acetylation and ubiquitination: Role in the control of protein stability
    • Caron, C., Boyault, C., and Khochbin, S. (2005) Regulatory cross-talk between lysine acetylation and ubiquitination: role in the control of protein stability. Bioessays 27, 408-415
    • (2005) Bioessays , vol.27 , pp. 408-415
    • Caron, C.1    Boyault, C.2    Khochbin, S.3
  • 9
    • 65349121777 scopus 로고    scopus 로고
    • Histone methylation and ubiquitination with their cross-talk and roles in gene expression and stability
    • Shukla, A., Chaurasia, P., and Bhaumik, S. R. (2009) Histone methylation and ubiquitination with their cross-talk and roles in gene expression and stability. Cell. Mol. Life Sci. 66, 1419-1433
    • (2009) Cell. Mol. Life Sci. , vol.66 , pp. 1419-1433
    • Shukla, A.1    Chaurasia, P.2    Bhaumik, S.R.3
  • 10
    • 79959381299 scopus 로고    scopus 로고
    • Cross talk between O-GlcNAcylation and phosphorylation: Roles in signaling, transcription, and chronic disease
    • Hart, G. W., Slawson, C., Ramirez-Correa, G., and Lagerlof, O. (2011) Cross talk between O-GlcNAcylation and phosphorylation: roles in signaling, transcription, and chronic disease. Annu. Rev. Biochem. 80, 825-858
    • (2011) Annu. Rev. Biochem. , vol.80 , pp. 825-858
    • Hart, G.W.1    Slawson, C.2    Ramirez-Correa, G.3    Lagerlof, O.4
  • 11
    • 84860184939 scopus 로고    scopus 로고
    • Bittersweet memories: Linking metabolism to epigenetics through O-GlcNAcylation
    • Hanover, J. A., Krause, M. W., and Love, D. C. (2012) Bittersweet memories: linking metabolism to epigenetics through O-GlcNAcylation. Nat. Rev. Mol. Cell Biol. 13, 312-321
    • (2012) Nat. Rev. Mol. Cell Biol. , vol.13 , pp. 312-321
    • Hanover, J.A.1    Krause, M.W.2    Love, D.C.3
  • 12
    • 0037300799 scopus 로고    scopus 로고
    • A role for N-acetylglucosamine as a nutrient sensor and mediator of insulin resistance
    • Wells, L., Vosseller, K., and Hart, G. W. (2003) A role for N-acetylglucosamine as a nutrient sensor and mediator of insulin resistance. Cell. Mol. Life Sci. 60, 222-228
    • (2003) Cell. Mol. Life Sci. , vol.60 , pp. 222-228
    • Wells, L.1    Vosseller, K.2    Hart, G.W.3
  • 14
    • 0035811072 scopus 로고    scopus 로고
    • O-linkage of N-acetylglucosamine to Sp1 activation domain inhibits its transcriptional capability
    • Yang, X., Su, K., Roos, M. D., Chang, Q., Paterson, A. J., and Kudlow, J. E. (2001) O-linkage of N-acetylglucosamine to Sp1 activation domain inhibits its transcriptional capability. Proc. Natl. Acad. Sci. U.S.A. 98, 6611-6616
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 6611-6616
    • Yang, X.1    Su, K.2    Roos, M.D.3    Chang, Q.4    Paterson, A.J.5    Kudlow, J.E.6
  • 15
    • 0037067659 scopus 로고    scopus 로고
    • Recruitment of O-GlcNAc transferase to promoters by corepressor mSin3A: Coupling protein OGlcNAcylation to transcriptional repression
    • Yang, X., Zhang, F., and Kudlow, J. E. (2002) Recruitment of O-GlcNAc transferase to promoters by corepressor mSin3A: coupling protein OGlcNAcylation to transcriptional repression. Cell 110, 69-80
    • (2002) Cell , vol.110 , pp. 69-80
    • Yang, X.1    Zhang, F.2    Kudlow, J.E.3
  • 17
    • 0021280147 scopus 로고
    • Topography and polypeptide distribution of terminal N-acetylglucosamine residues on the surfaces of intact lymphocytes. Evidence for O-linked GlcNAc
    • Torres, C. R., and Hart, G. W. (1984) Topography and polypeptide distribution of terminal N-acetylglucosamine residues on the surfaces of intact lymphocytes. Evidence for O-linked GlcNAc. J. Biol. Chem. 259, 3308-3317
    • (1984) J. Biol. Chem. , vol.259 , pp. 3308-3317
    • Torres, C.R.1    Hart, G.W.2
  • 18
    • 78049390185 scopus 로고    scopus 로고
    • O-GlcNAc transferase regulates mitotic chromatin dynamics
    • Sakabe, K., and Hart, G. W. (2010) O-GlcNAc transferase regulates mitotic chromatin dynamics. J. Biol. Chem. 285, 34460-34468
    • (2010) J. Biol. Chem. , vol.285 , pp. 34460-34468
    • Sakabe, K.1    Hart, G.W.2
  • 19
    • 84867650919 scopus 로고    scopus 로고
    • Modification of RelA by O-linked N-acetylglucosamine links glucose metabolism to NF-kappaB acetylation and transcription
    • Allison, D. F., Wamsley, J. J., Kumar, M., Li, D., Gray, L. G., Hart, G. W., Jones, D. R., and Mayo, M. W. (2012) Modification of RelA by O-linked N-acetylglucosamine links glucose metabolism to NF-kappaB acetylation and transcription. Proc. Natl. Acad. Sci. U.S.A. 109, 16888-16893
    • (2012) Proc. Natl. Acad. Sci. U.S.A. , vol.109 , pp. 16888-16893
    • Allison, D.F.1    Wamsley, J.J.2    Kumar, M.3    Li, D.4    Gray, L.G.5    Hart, G.W.6    Jones, D.R.7    Mayo, M.W.8
  • 22
    • 0034703742 scopus 로고    scopus 로고
    • P53: Death star
    • Vousden, K. H. (2000) p53: death star. Cell 103, 691-694
    • (2000) Cell , vol.103 , pp. 691-694
    • Vousden, K.H.1
  • 23
    • 43949107925 scopus 로고    scopus 로고
    • SnapShot: P53 posttranslational modifications
    • Kruse, J. P., and Gu, W. (2008) SnapShot: p53 posttranslational modifications. Cell 133, 930-30.e1
    • (2008) Cell , vol.133
    • Kruse, J.P.1    Gu, W.2
  • 24
    • 33749160125 scopus 로고    scopus 로고
    • Modification of p53 with O-linked N-acetylglucosamine regulates p53 activity and stability
    • Yang, W. H., Kim, J. E., Nam, H. W., Ju, J. W., Kim, H. S., Kim, Y. S., and Cho, J. W. (2006) Modification of p53 with O-linked N-acetylglucosamine regulates p53 activity and stability. Nat. Cell Biol. 8, 1074-1083
    • (2006) Nat. Cell Biol. , vol.8 , pp. 1074-1083
    • Yang, W.H.1    Kim, J.E.2    Nam, H.W.3    Ju, J.W.4    Kim, H.S.5    Kim, Y.S.6    Cho, J.W.7
  • 25
  • 26
    • 58149115086 scopus 로고    scopus 로고
    • Proteomic approach to the identification of novel delta-lactoferrin target genes: Characterization of DcpS, an mRNA scavenger decapping enzyme
    • Mariller, C., Hardiville, S., Hoedt, E., Benaissa, M., Mazurier, J., and Pierce, A. (2009) Proteomic approach to the identification of novel delta-lactoferrin target genes: characterization of DcpS, an mRNA scavenger decapping enzyme. Biochimie (Paris) 91, 109-122
    • (2009) Biochimie (Paris) , vol.91 , pp. 109-122
    • Mariller, C.1    Hardiville, S.2    Hoedt, E.3    Benaissa, M.4    Mazurier, J.5    Pierce, A.6
  • 27
    • 77953500021 scopus 로고    scopus 로고
    • O-GlcNAcylation/phosphorylation cycling at Ser10 controls both transcriptional activity and stability of delta-lactoferrin
    • Hardiville, S., Hoedt, E., Mariller, C., Benaissa, M., and Pierce, A. (2010) O-GlcNAcylation/phosphorylation cycling at Ser10 controls both transcriptional activity and stability of delta-lactoferrin. J. Biol. Chem. 285, 19205-19218
    • (2010) J. Biol. Chem. , vol.285 , pp. 19205-19218
    • Hardiville, S.1    Hoedt, E.2    Mariller, C.3    Benaissa, M.4    Pierce, A.5
  • 28
    • 33645302628 scopus 로고    scopus 로고
    • The epithelial- mesenchymal transition: New insights in signaling, development, and disease
    • Lee, J. M., Dedhar, S., Kalluri, R., and Thompson, E. W. (2006) The epithelial- mesenchymal transition: new insights in signaling, development, and disease. J. Cell Biol. 172, 973-981
    • (2006) J. Cell Biol. , vol.172 , pp. 973-981
    • Lee, J.M.1    Dedhar, S.2    Kalluri, R.3    Thompson, E.W.4
  • 31
    • 33846018559 scopus 로고    scopus 로고
    • Estrogen receptor-beta: Recent lessons from in vivo studies
    • Harris, H. A. (2007) Estrogen receptor-beta: recent lessons from in vivo studies. Mol. Endocrinol. 21, 1-13
    • (2007) Mol. Endocrinol. , vol.21 , pp. 1-13
    • Harris, H.A.1
  • 32
    • 0035971067 scopus 로고    scopus 로고
    • Alternative O-glycosylation/O-phosphorylation of serine-16 in murine estrogen receptor beta: Post-translational regulation of turnover and transactivation activity
    • Cheng, X., and Hart, G. W. (2001) Alternative O-glycosylation/O- phosphorylation of serine-16 in murine estrogen receptor beta: post-translational regulation of turnover and transactivation activity. J. Biol. Chem. 276, 10570-10575
    • (2001) J. Biol. Chem. , vol.276 , pp. 10570-10575
    • Cheng, X.1    Hart, G.W.2
  • 33
    • 70349186117 scopus 로고    scopus 로고
    • Protein kinase CK2 in health and disease: From birth to death: The role of protein kinase CK2 in the regulation of cell proliferation and survival
    • St-Denis, N. A., and Litchfield, D. W. (2009) Protein kinase CK2 in health and disease: from birth to death: the role of protein kinase CK2 in the regulation of cell proliferation and survival. Cell. Mol. Life Sci. 66, 1817-1829
    • (2009) Cell. Mol. Life Sci. , vol.66 , pp. 1817-1829
    • St-Denis, N.A.1    Litchfield, D.W.2
  • 37
    • 40449128605 scopus 로고    scopus 로고
    • Hepatic glucose sensing via the CREB coactivator CRTC2
    • Dentin, R., Hedrick, S., Xie, J., Yates, J., 3rd, and Montminy, M. (2008) Hepatic glucose sensing via the CREB coactivator CRTC2. Science 319, 1402-1405
    • (2008) Science , vol.319 , pp. 1402-1405
    • Dentin, R.1    Hedrick, S.2    Xie, J.3    Yates III, J.4    Montminy, M.5
  • 38
    • 79953210362 scopus 로고    scopus 로고
    • Regulation of PGC-1alpha, a nodal regulator of mitochondrial biogenesis
    • Fernandez-Marcos, P. J., and Auwerx, J. (2011) Regulation of PGC-1alpha, a nodal regulator of mitochondrial biogenesis. Am. J. Clin. Nutr. 93, 884S-890S
    • (2011) Am. J. Clin. Nutr. , vol.93
    • Fernandez-Marcos, P.J.1    Auwerx, J.2
  • 40
    • 71749110779 scopus 로고    scopus 로고
    • The deubiquitinating enzyme BAP1 regulates cell growth via interaction with HCF-1
    • Machida, Y. J., Machida, Y., Vashisht, A. A., Wohlschlegel, J. A., and Dutta, A. (2009) The deubiquitinating enzyme BAP1 regulates cell growth via interaction with HCF-1. J. Biol. Chem. 284, 34179-34188
    • (2009) J. Biol. Chem. , vol.284 , pp. 34179-34188
    • Machida, Y.J.1    Machida, Y.2    Vashisht, A.A.3    Wohlschlegel, J.A.4    Dutta, A.5
  • 41
    • 84869036539 scopus 로고    scopus 로고
    • Circadian topology of metabolism
    • Bass, J. (2012) Circadian topology of metabolism. Nature 491, 348-356
    • (2012) Nature , vol.491 , pp. 348-356
    • Bass, J.1
  • 42
    • 33749031807 scopus 로고    scopus 로고
    • Molecular components of the mammalian circadian clock
    • Ko, C. H., and Takahashi, J. S. (2006) Molecular components of the mammalian circadian clock. Hum. Mol. Genet. 15 Spec No 2, R271-R277
    • (2006) Hum. Mol. Genet. 15 Spec , vol.15 , Issue.SPEC. 2
    • Ko, C.H.1    Takahashi, J.S.2
  • 43
    • 78649687209 scopus 로고    scopus 로고
    • Circadian integration of metabolism and energetics
    • Bass, J., and Takahashi, J. S. (2010) Circadian integration of metabolism and energetics. Science 330, 1349-1354
    • (2010) Science , vol.330 , pp. 1349-1354
    • Bass, J.1    Takahashi, J.S.2
  • 44
    • 84863230299 scopus 로고    scopus 로고
    • A role for O-GlcNAcylation in setting circadian clock speed
    • Kim, E. Y., Jeong, E. H., Park, S., Jeong, H. J., Edery, I., and Cho, J. W. (2012) A role for O-GlcNAcylation in setting circadian clock speed. Genes Dev. 26, 490-502
    • (2012) Genes Dev. , vol.26 , pp. 490-502
    • Kim, E.Y.1    Jeong, E.H.2    Park, S.3    Jeong, H.J.4    Edery, I.5    Cho, J.W.6
  • 48
    • 38449087713 scopus 로고    scopus 로고
    • ChREBP, a transcriptional regulator of glucose and lipid metabolism
    • Postic, C., Dentin, R., Denechaud, P. D., and Girard, J. (2007) ChREBP, a transcriptional regulator of glucose and lipid metabolism. Annu. Rev. Nutr. 27, 179-192
    • (2007) Annu. Rev. Nutr. , vol.27 , pp. 179-192
    • Postic, C.1    Dentin, R.2    Denechaud, P.D.3    Girard, J.4
  • 51
    • 34347374872 scopus 로고    scopus 로고
    • Intermediate filament scaffolds fulfill mechanical, organizational, and signaling functions in the cytoplasm
    • Kim, S., and Coulombe, P. A. (2007) Intermediate filament scaffolds fulfill mechanical, organizational, and signaling functions in the cytoplasm. Genes Dev. 21, 1581-1597
    • (2007) Genes Dev. , vol.21 , pp. 1581-1597
    • Kim, S.1    Coulombe, P.A.2
  • 52
    • 33745873555 scopus 로고    scopus 로고
    • "Heads and tails" of intermediate filament phosphorylation: Multiple sites and functional insights
    • Omary, M. B., Ku, N. O., Tao, G. Z., Toivola, D. M., and Liao, J. (2006) "Heads and tails" of intermediate filament phosphorylation: multiple sites and functional insights. Trends Biochem. Sci. 31, 383-394
    • (2006) Trends Biochem. Sci. , vol.31 , pp. 383-394
    • Omary, M.B.1    Ku, N.O.2    Tao, G.Z.3    Toivola, D.M.4    Liao, J.5
  • 53
    • 77958616531 scopus 로고    scopus 로고
    • O-GlcNAcylation determines the solubility, filament organization, and stability of keratins 8 and 18
    • Srikanth, B., Vaidya, M. M., and Kalraiya, R. D. (2010) O-GlcNAcylation determines the solubility, filament organization, and stability of keratins 8 and 18. J. Biol. Chem. 285, 34062-34071
    • (2010) J. Biol. Chem. , vol.285 , pp. 34062-34071
    • Srikanth, B.1    Vaidya, M.M.2    Kalraiya, R.D.3
  • 56
    • 0037544034 scopus 로고    scopus 로고
    • A glycosylation site, 60SGTS63, of p67 is required for its ability to regulate the phosphorylation and activity of eukaryotic initiation factor 2alpha
    • Datta, R., Choudhury, P., Ghosh, A., and Datta, B. (2003) A glycosylation site, 60SGTS63, of p67 is required for its ability to regulate the phosphorylation and activity of eukaryotic initiation factor 2alpha. Biochemistry 42, 5453-5460
    • (2003) Biochemistry , vol.42 , pp. 5453-5460
    • Datta, R.1    Choudhury, P.2    Ghosh, A.3    Datta, B.4
  • 57
    • 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., and Reginato, M. J. (2010) Nutrient sensor O-GlcNAc transferase regulates breast cancer tumorigenesis through targeting of the oncogenic transcription factor FoxM1. Oncogene 29, 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
  • 58
    • 33744953426 scopus 로고    scopus 로고
    • Stabilization of plakoglobin and enhanced keratinocyte cell-cell adhesion by intracellular O-glycosylation
    • Hu, P., Berkowitz, P., Madden, V. J., and Rubenstein, D. S. (2006) Stabilization of plakoglobin and enhanced keratinocyte cell-cell adhesion by intracellular O-glycosylation. J. Biol. Chem. 281, 12786-12791
    • (2006) J. Biol. Chem. , vol.281 , pp. 12786-12791
    • Hu, P.1    Berkowitz, P.2    Madden, V.J.3    Rubenstein, D.S.4
  • 59
    • 0030907389 scopus 로고    scopus 로고
    • Reduced O glycosylation of Sp1 is associated with increased proteasome susceptibility
    • Han, I., and Kudlow, J. E. (1997) Reduced O glycosylation of Sp1 is associated with increased proteasome susceptibility. Mol. Cell. Biol. 17, 2550-2558
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 2550-2558
    • Han, I.1    Kudlow, J.E.2
  • 60
    • 84862506186 scopus 로고    scopus 로고
    • Cardiac transcription factor Nkx2.5 is downregulated under excessive OGlcNAcylation condition
    • Kim, H. S., Woo, J. S., Joo, H. J., and Moon, W. K. (2012) Cardiac transcription factor Nkx2.5 is downregulated under excessive OGlcNAcylation condition. PLoS One 7, e38053
    • (2012) PLoS One , vol.7
    • Kim, H.S.1    Woo, J.S.2    Joo, H.J.3    Moon, W.K.4
  • 61
    • 78650969834 scopus 로고    scopus 로고
    • Hexosamines stimulate apoptosis by altering SIRT1 action and levels in rodent pancreatic beta-cells
    • Lafontaine-Lacasse, M., Dore, G., and Picard, F. (2011) Hexosamines stimulate apoptosis by altering SIRT1 action and levels in rodent pancreatic beta-cells. J. Endocrinol. 208, 41-49
    • (2011) J. Endocrinol. , vol.208 , pp. 41-49
    • Lafontaine-Lacasse, M.1    Dore, G.2    Picard, F.3
  • 62
    • 40849106789 scopus 로고    scopus 로고
    • Histone ubiquitination: Triggering gene activity
    • Weake, V. M., and Workman, J. L. (2008) Histone ubiquitination: triggering gene activity. Mol. Cell 29, 653-663
    • (2008) Mol. Cell , vol.29 , pp. 653-663
    • Weake, V.M.1    Workman, J.L.2
  • 63
    • 78650447665 scopus 로고    scopus 로고
    • Beta-N-acetylglucosamine (O-GlcNAc) is part of the histone code
    • Sakabe, K., Wang, Z., and Hart, G. W. (2010) Beta-N-acetylglucosamine (O-GlcNAc) is part of the histone code. Proc. Natl. Acad. Sci. U.S.A. 107, 19915-19920
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 19915-19920
    • Sakabe, K.1    Wang, Z.2    Hart, G.W.3
  • 65
    • 80054818714 scopus 로고    scopus 로고
    • Modification of histones by sugar beta-N-acetylglucosamine (GlcNAc) occurs on multiple residues, including histone H3 serine 10, and is cell cycleregulated
    • Zhang, S., Roche, K., Nasheuer, H. P., and Lowndes, N. F. (2011) Modification of histones by sugar beta-N-acetylglucosamine (GlcNAc) occurs on multiple residues, including histone H3 serine 10, and is cell cycleregulated. J. Biol. Chem. 286, 37483-37495
    • (2011) J. Biol. Chem. , vol.286 , pp. 37483-37495
    • Zhang, S.1    Roche, K.2    Nasheuer, H.P.3    Lowndes, N.F.4
  • 66
    • 84859512121 scopus 로고    scopus 로고
    • Beta-N-acetylglucosamine (O-GlcNAc) is a novel regulator of mitosis-specific phosphorylations on histone H3
    • Fong, J. J., Nguyen, B. L., Bridger, R., Medrano, E. E., Wells, L., Pan, S., and Sifers, R. N. (2012) beta-N-acetylglucosamine (O-GlcNAc) is a novel regulator of mitosis-specific phosphorylations on histone H3. J. Biol. Chem. 287, 12195-12203
    • (2012) J. Biol. Chem. , vol.287 , pp. 12195-12203
    • Fong, J.J.1    Nguyen, B.L.2    Bridger, R.3    Medrano, E.E.4    Wells, L.5    Pan, S.6    Sifers, R.N.7
  • 67
    • 84872953223 scopus 로고    scopus 로고
    • TET2 promotes histone O-GlcNAcylation during gene transcription
    • Chen, Q., Chen, Y., Bian, C., Fujiki, R., and Yu, X. (2013) TET2 promotes histone O-GlcNAcylation during gene transcription. Nature 493, 561-564
    • (2013) Nature , vol.493 , pp. 561-564
    • Chen, Q.1    Chen, Y.2    Bian, C.3    Fujiki, R.4    Yu, X.5
  • 69
    • 0345357692 scopus 로고    scopus 로고
    • 26S proteasome subunits are O-linked N-acetylglucosaminemodified in Drosophila melanogaster
    • Sumegi, M., Hunyadi-Gulyas, E., Medzihradszky, K. F., and Udvardy, A. (2003) 26S proteasome subunits are O-linked N-acetylglucosaminemodified in Drosophila melanogaster. Biochem. Biophys. Res. Commun. 312, 1284-1289
    • (2003) Biochem. Biophys. Res. Commun. , vol.312 , pp. 1284-1289
    • Sumegi, M.1    Hunyadi-Gulyas, E.2    Medzihradszky, K.F.3    Udvardy, A.4
  • 70
    • 0346965700 scopus 로고    scopus 로고
    • O-GlcNAc modification is an endogenous inhibitor of the proteasome
    • Zhang, F., Su, K., Yang, X., Bowe, D. B., Paterson, A. J., and Kudlow, J. E. (2003) O-GlcNAc modification is an endogenous inhibitor of the proteasome. Cell 115, 715-725
    • (2003) Cell , vol.115 , pp. 715-725
    • Zhang, F.1    Su, K.2    Yang, X.3    Bowe, D.B.4    Paterson, A.J.5    Kudlow, J.E.6
  • 71
    • 79961138782 scopus 로고    scopus 로고
    • A lipid-droplet-targeted O-GlcNAcase isoform is a key regulator of the proteasome
    • Keembiyehetty, C. N., Krzeslak, A., Love, D. C., and Hanover, J. A. (2011) A lipid-droplet-targeted O-GlcNAcase isoform is a key regulator of the proteasome. J. Cell Sci. 124, 2851-2860
    • (2011) J. Cell Sci. , vol.124 , pp. 2851-2860
    • Keembiyehetty, C.N.1    Krzeslak, A.2    Love, D.C.3    Hanover, J.A.4
  • 75
    • 78650034178 scopus 로고    scopus 로고
    • Ubiquitin/proteasome pathway impairment in neurodegeneration: Therapeutic implications
    • Huang, Q., and Figueiredo-Pereira, M. E. (2010) Ubiquitin/proteasome pathway impairment in neurodegeneration: therapeutic implications. Apoptosis 15, 1292-1311
    • (2010) Apoptosis , vol.15 , pp. 1292-1311
    • Huang, Q.1    Figueiredo-Pereira, M.E.2
  • 76
    • 84856977664 scopus 로고    scopus 로고
    • The ubiquitin proteasome system in neurodegenerative diseases: Culprit, accomplice or victim?
    • Dennissen, F. J., Kholod, N., and van Leeuwen, F. W. (2012) The ubiquitin proteasome system in neurodegenerative diseases: culprit, accomplice or victim? Prog. Neurobiol. 96, 190-207
    • (2012) Prog. Neurobiol. , Issue.96 , pp. 190-207
    • Dennissen, F.J.1    Kholod, N.2    Van Leeuwen, F.W.3
  • 77
    • 84864233715 scopus 로고    scopus 로고
    • Temporal separation of aggregation and ubiquitination during early inclusion formation in transgenic mice carrying the Huntington's disease mutation
    • Gong, B., Kielar, C., and Morton, A. J. (2012) Temporal separation of aggregation and ubiquitination during early inclusion formation in transgenic mice carrying the Huntington's disease mutation. PLoS One 7, e41450
    • (2012) PLoS One , vol.7
    • Gong, B.1    Kielar, C.2    Morton, A.J.3
  • 78
    • 84867903851 scopus 로고    scopus 로고
    • O-GlcNAc cycling modulates neurodegeneration
    • Gong, C. X., Liu, F., and Iqbal, K. (2012) O-GlcNAc cycling modulates neurodegeneration. Proc. Natl. Acad. Sci. U.S.A. 109, 17319-17320
    • (2012) Proc. Natl. Acad. Sci. U.S.A. , vol.109 , pp. 17319-17320
    • Gong, C.X.1    Liu, F.2    Iqbal, K.3
  • 79
    • 84860487289 scopus 로고    scopus 로고
    • Reduced protein O-glycosylation in the nervous system of the mutant SOD1 transgenic mouse model of amyotrophic lateral sclerosis
    • Shan, X., Vocadlo, D. J., and Krieger, C. (2012) Reduced protein O-glycosylation in the nervous system of the mutant SOD1 transgenic mouse model of amyotrophic lateral sclerosis. Neurosci. Lett. 516, 296-301
    • (2012) Neurosci. Lett. , vol.516 , pp. 296-301
    • Shan, X.1    Vocadlo, D.J.2    Krieger, C.3
  • 81
    • 84867908726 scopus 로고    scopus 로고
    • O-GlcNAc cycling mutants modulate proteotoxicity in Caenorhabditis elegans models of human neurodegenerative diseases
    • Wang, P., Lazarus, B. D., Forsythe, M. E., Love, D. C., Krause, M. W., and Hanover, J. A. (2012) O-GlcNAc cycling mutants modulate proteotoxicity in Caenorhabditis elegans models of human neurodegenerative diseases. Proc. Natl. Acad. Sci. U.S.A. 109, 17669-17674
    • (2012) Proc. Natl. Acad. Sci. U.S.A. , vol.109 , pp. 17669-17674
    • Wang, P.1    Lazarus, B.D.2    Forsythe, M.E.3    Love, D.C.4    Krause, M.W.5    Hanover, J.A.6
  • 82
    • 84863454687 scopus 로고    scopus 로고
    • Ubiquitylation in immune disorders and cancer: From molecular mechanisms to therapeutic implications
    • Fulda, S., Rajalingam, K., and Dikic, I. (2012) Ubiquitylation in immune disorders and cancer: from molecular mechanisms to therapeutic implications. EMBO Mol. Med. 4, 545-556
    • (2012) EMBO Mol. Med. , vol.4 , pp. 545-556
    • Fulda, S.1    Rajalingam, K.2    Dikic, I.3
  • 84
    • 80052068559 scopus 로고    scopus 로고
    • O-GlcNAc signalling: Implications for cancer cell biology
    • Slawson, C., and Hart, G. W. (2011) O-GlcNAc signalling: implications for cancer cell biology. Nat. Rev. Cancer 11, 678-684
    • (2011) Nat. Rev. Cancer , vol.11 , pp. 678-684
    • Slawson, C.1    Hart, G.W.2
  • 85
    • 44949231368 scopus 로고    scopus 로고
    • Genome-wide and functional annotation of human E3 ubiquitin ligases identifies MULAN, a mitochondrial E3 that regulates the organelle's dynamics and signaling
    • Li, W., Bengtson, M. H., Ulbrich, A., Matsuda, A., Reddy, V. A., Orth, A., Chanda, S. K., Batalov, S., and Joazeiro, C. A. (2008) Genome-wide and functional annotation of human E3 ubiquitin ligases identifies MULAN, a mitochondrial E3 that regulates the organelle's dynamics and signaling. PLoS One 3, e1487
    • (2008) PLoS One , vol.3
    • Li, W.1    Bengtson, M.H.2    Ulbrich, A.3    Matsuda, A.4    Reddy, V.A.5    Orth, A.6    Chanda, S.K.7    Batalov, S.8    Joazeiro, C.A.9
  • 89
    • 84873350431 scopus 로고    scopus 로고
    • Proteome wide purification and identification of O-GlcNAc-modified proteins using click chemistry and mass spectrometry
    • Hahne, H., Sobotzki, N., Nyberg, T., Helm, D., Borodkin, V. S., van Aalten, D. M., Agnew, B., and Kuster, B. (2013) Proteome wide purification and identification of O-GlcNAc-modified proteins using click chemistry and mass spectrometry. J. Proteome Res. 12, 927-936
    • (2013) J. Proteome Res. , vol.12 , pp. 927-936
    • Hahne, H.1    Sobotzki, N.2    Nyberg, T.3    Helm, D.4    Borodkin, V.S.5    Van Aalten, D.M.6    Agnew, B.7    Kuster, B.8
  • 94
    • 79957694784 scopus 로고    scopus 로고
    • Chemical reporters for fluorescent detection and identification of O-GlcNAc-modified proteins reveal glycosylation of the ubiquitin ligase NEDD4-1
    • Zaro, B. W., Yang, Y. Y., Hang, H. C., and Pratt, M. R. (2011) Chemical reporters for fluorescent detection and identification of O-GlcNAc-modified proteins reveal glycosylation of the ubiquitin ligase NEDD4-1. Proc. Natl. Acad. Sci. U.S.A. 108, 8146-8151
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 8146-8151
    • Zaro, B.W.1    Yang, Y.Y.2    Hang, H.C.3    Pratt, M.R.4
  • 95
    • 84867167595 scopus 로고    scopus 로고
    • Discovery of O-GlcNAc-modified proteins in published large-scale proteome data
    • Hahne, H., Moghaddas Gholami, A., and Kuster, B. (2012) Discovery of O-GlcNAc-modified proteins in published large-scale proteome data. Mol. Cell. Proteomics 11, 843-850
    • (2012) Mol. Cell. Proteomics , vol.11 , pp. 843-850
    • Hahne, H.1    Moghaddas Gholami, A.2    Kuster, B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.