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Volumn 8, Issue 5, 2013, Pages

Substrate Specificity Provides Insights into the Sugar Donor Recognition Mechanism of O-GlcNAc Transferase (OGT)

Author keywords

[No Author keywords available]

Indexed keywords

CARBOHYDRATE DERIVATIVE; CASEIN KINASE II; N ACETYLGLUCOSAMINYLTRANSFERASE; OXYGEN; SUGAR DONOR; UNCLASSIFIED DRUG; URIDINE DIPHOSPHATE 4 DEOXY N ACETYLGLUCOSAMINE; URIDINE DIPHOSPHATE 6 DEOXY N ACETYLGLUCOSAMINE; URIDINE DIPHOSPHATE N ACETYLGLUCOSAMINE;

EID: 84877960116     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0063452     Document Type: Article
Times cited : (30)

References (43)
  • 1
    • 0021280147 scopus 로고
    • Topography and polypeptide distribution of terminal N-acetylglucosamine residues on the surfaces of intact lymphocytes. Evidence for O-linked GlcNAc
    • Torres CR, Hart GW, (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
  • 2
    • 34247583996 scopus 로고    scopus 로고
    • Cycling of O-linked beta-N-acetylglucosamine on nucleocytoplasmic proteins
    • Hart GW, Housley MP, Slawson C, (2007) Cycling of O-linked beta-N-acetylglucosamine on nucleocytoplasmic proteins. Nature 446: 1017-1022.
    • (2007) Nature , vol.446 , pp. 1017-1022
    • Hart, G.W.1    Housley, M.P.2    Slawson, C.3
  • 3
    • 0035937586 scopus 로고    scopus 로고
    • Glycosylation of nucleocytoplasmic proteins: signal transduction and O-GlcNAc
    • Wells L, Vosseller K, Hart GW, (2001) Glycosylation of nucleocytoplasmic proteins: signal transduction and O-GlcNAc. Science 291: 2376-2378.
    • (2001) Science , vol.291 , pp. 2376-2378
    • Wells, L.1    Vosseller, K.2    Hart, G.W.3
  • 4
    • 33745272509 scopus 로고    scopus 로고
    • Cell signaling, the essential role of O-GlcNAc!
    • Zachara NE, Hart GW, (2006) Cell signaling, the essential role of O-GlcNAc! Biochim Biophys Acta. 1761: 599-617.
    • (2006) Biochim Biophys Acta , vol.1761 , pp. 599-617
    • Zachara, N.E.1    Hart, G.W.2
  • 5
    • 77949769388 scopus 로고    scopus 로고
    • O-linked beta-N-acetylglucosamine (O-GlcNAc): Extensive crosstalk with phosphorylation to regulate signaling and transcription in response to nutrients and stress
    • Butkinaree C, Park K, Hart GW, (2010) O-linked beta-N-acetylglucosamine (O-GlcNAc): Extensive crosstalk with phosphorylation to regulate signaling and transcription in response to nutrients and stress. Biochimica Et Biophysica Acta-General Subjects 1800: 96-106.
    • (2010) Biochimica Et Biophysica Acta-General Subjects , vol.1800 , pp. 96-106
    • Butkinaree, C.1    Park, K.2    Hart, G.W.3
  • 6
    • 0032734974 scopus 로고    scopus 로고
    • O-GlcNAc and the control of gene expression
    • Comer FI, Hart GW, (1999) O-GlcNAc and the control of gene expression. Biochim Biophys Acta 1473: 161-171.
    • (1999) Biochim Biophys Acta , vol.1473 , pp. 161-171
    • Comer, F.I.1    Hart, G.W.2
  • 7
    • 84857193629 scopus 로고    scopus 로고
    • Dynamic O-GlcNAc modification regulates CREB-mediated gene expression and memory formation
    • Rexach JE, Clark PM, Mason DE, Neve RL, Peters EC, et al. (2012) Dynamic O-GlcNAc modification regulates CREB-mediated gene expression and memory formation. Nat Chem Biol 8: 253-261.
    • (2012) Nat Chem Biol , vol.8 , pp. 253-261
    • Rexach, J.E.1    Clark, P.M.2    Mason, D.E.3    Neve, R.L.4    Peters, E.C.5
  • 9
    • 79751525993 scopus 로고    scopus 로고
    • O-GlcNAcylation is a novel regulator of lung and colon cancer malignancy
    • Mi W, Gu Y, Han C, Liu H, Fan Q, et al. (2011) O-GlcNAcylation is a novel regulator of lung and colon cancer malignancy. Biochim Biophys Acta 1812: 514-519.
    • (2011) Biochim Biophys Acta , vol.1812 , pp. 514-519
    • Mi, W.1    Gu, Y.2    Han, C.3    Liu, H.4    Fan, Q.5
  • 11
    • 84859484538 scopus 로고    scopus 로고
    • Critical role of O-Linked beta-N-acetylglucosamine transferase in prostate cancer invasion, angiogenesis, and metastasis
    • Lynch TP, Ferrer CM, Jackson SR, Shahriari KS, Vosseller K, et al. (2012) Critical role of O-Linked beta-N-acetylglucosamine transferase in prostate cancer invasion, angiogenesis, and metastasis. J Biol Chem 287: 11070-11081.
    • (2012) J Biol Chem , vol.287 , pp. 11070-11081
    • Lynch, T.P.1    Ferrer, C.M.2    Jackson, S.R.3    Shahriari, K.S.4    Vosseller, K.5
  • 12
    • 33846488647 scopus 로고    scopus 로고
    • Elevation of the post-translational modification of proteins by O-linked N-acetylglucosamine leads to deterioration of the glucose-stimulated insulin secretion in the pancreas of diabetic Goto-Kakizaki rats
    • Akimoto Y, Hart GW, Wells L, Vosseller K, Yamamoto K, et al. (2007) Elevation of the post-translational modification of proteins by O-linked N-acetylglucosamine leads to deterioration of the glucose-stimulated insulin secretion in the pancreas of diabetic Goto-Kakizaki rats. Glycobiology 17: 127-140.
    • (2007) Glycobiology , vol.17 , pp. 127-140
    • Akimoto, Y.1    Hart, G.W.2    Wells, L.3    Vosseller, K.4    Yamamoto, K.5
  • 13
    • 0029120744 scopus 로고
    • O-linked N-acetylglucosamine is upregulated in Alzheimer brains
    • Griffith LS, Schmitz B, (1995) O-linked N-acetylglucosamine is upregulated in Alzheimer brains. Biochem Biophys Res Commun 213: 424-431.
    • (1995) Biochem Biophys Res Commun , vol.213 , pp. 424-431
    • Griffith, L.S.1    Schmitz, B.2
  • 14
    • 79959381299 scopus 로고    scopus 로고
    • Cross talk between O-GlcNAcylation and phosphorylation: roles in signaling, transcription, and chronic disease
    • Hart GW, Slawson C, Ramirez-Correa G, 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
  • 15
    • 0037440370 scopus 로고    scopus 로고
    • Mitochondrial and nucleocytoplasmic isoforms of O-linked GlcNAc transferase encoded by a single mammalian gene
    • Hanover JA, Yu S, Lubas WB, Shin SH, Ragano-Caracciola M, et al. (2003) Mitochondrial and nucleocytoplasmic isoforms of O-linked GlcNAc transferase encoded by a single mammalian gene. Arch Biochem Biophys 409: 287-297.
    • (2003) Arch Biochem Biophys , vol.409 , pp. 287-297
    • Hanover, J.A.1    Yu, S.2    Lubas, W.B.3    Shin, S.H.4    Ragano-Caracciola, M.5
  • 16
    • 0033527739 scopus 로고    scopus 로고
    • Regulation of a cytosolic and nuclear O-GlcNAc transferase. Role of the tetratricopeptide repeats
    • Kreppel LK, Hart GW, (1999) Regulation of a cytosolic and nuclear O-GlcNAc transferase. Role of the tetratricopeptide repeats. J Biol Chem 274: 32015-32022.
    • (1999) J Biol Chem , vol.274 , pp. 32015-32022
    • Kreppel, L.K.1    Hart, G.W.2
  • 17
    • 0034646669 scopus 로고    scopus 로고
    • Functional expression of O-linked GlcNAc transferase - Domain structure and substrate specificity
    • Lubas WA, Hanover JA, (2000) Functional expression of O-linked GlcNAc transferase- Domain structure and substrate specificity. Journal of Biological Chemistry 275: 10983-10988.
    • (2000) Journal of Biological Chemistry , vol.275 , pp. 10983-10988
    • Lubas, W.A.1    Hanover, J.A.2
  • 18
    • 0042090275 scopus 로고    scopus 로고
    • Roles of the tetratricopeptide repeat domain in O-GlcNAc transferase targeting and protein substrate specificity
    • Iyer SPN, Hart GW, (2003) Roles of the tetratricopeptide repeat domain in O-GlcNAc transferase targeting and protein substrate specificity. Journal of Biological Chemistry 278: 24608-24616.
    • (2003) Journal of Biological Chemistry , vol.278 , pp. 24608-24616
    • Iyer, S.P.N.1    Hart, G.W.2
  • 19
    • 0030959555 scopus 로고    scopus 로고
    • Dynamic glycosylation of nuclear and cytosolic proteins. Cloning and characterization of a unique O-GlcNAc transferase with multiple tetratricopeptide repeats
    • Kreppel LK, Blomberg MA, Hart GW, (1997) Dynamic glycosylation of nuclear and cytosolic proteins. Cloning and characterization of a unique O-GlcNAc transferase with multiple tetratricopeptide repeats. J Biol Chem 272: 9308-9315.
    • (1997) J Biol Chem , vol.272 , pp. 9308-9315
    • Kreppel, L.K.1    Blomberg, M.A.2    Hart, G.W.3
  • 20
    • 27444447560 scopus 로고    scopus 로고
    • Mutational analysis of the catalytic domain of O-linked N-acetylglucosaminyl transferase
    • Lazarus BD, Roos MD, Hanover JA, (2005) Mutational analysis of the catalytic domain of O-linked N-acetylglucosaminyl transferase. Journal of Biological Chemistry 280: 35537-35544.
    • (2005) Journal of Biological Chemistry , vol.280 , pp. 35537-35544
    • Lazarus, B.D.1    Roos, M.D.2    Hanover, J.A.3
  • 21
    • 79251611901 scopus 로고    scopus 로고
    • Structure of human O-GlcNAc transferase and its complex with a peptide substrate
    • Lazarus MB, Nam Y, Jiang J, Sliz P, Walker S, (2011) Structure of human O-GlcNAc transferase and its complex with a peptide substrate. Nature 469: 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
  • 22
    • 0035976715 scopus 로고    scopus 로고
    • Homology between O-linked GlcNAc transferases and proteins of the glycogen phosphorylase superfamily
    • Wrabl JO, Grishin NV, (2001) Homology between O-linked GlcNAc transferases and proteins of the glycogen phosphorylase superfamily. J Mol Biol 314: 365-374.
    • (2001) J Mol Biol , vol.314 , pp. 365-374
    • Wrabl, J.O.1    Grishin, N.V.2
  • 23
    • 4744341309 scopus 로고    scopus 로고
    • The superhelical TPR-repeat domain of O-linked GlcNAc transferase exhibits structural similarities to importin alpha
    • Jinek M, Rehwinkel J, Lazarus BD, Izaurralde E, Hanover JA, et al. (2004) The superhelical TPR-repeat domain of O-linked GlcNAc transferase exhibits structural similarities to importin alpha. Nat Struct Mol Biol 11: 1001-1007.
    • (2004) Nat Struct Mol Biol , vol.11 , pp. 1001-1007
    • Jinek, M.1    Rehwinkel, J.2    Lazarus, B.D.3    Izaurralde, E.4    Hanover, J.A.5
  • 24
    • 46449085222 scopus 로고    scopus 로고
    • Structure of an O-GlcNAc transferase homolog provides insight into intracellular glycosylation
    • Martinez-Fleites C, Macauley MS, He Y, Shen DL, Vocadlo DJ, et al. (2008) Structure of an O-GlcNAc transferase homolog provides insight into intracellular glycosylation. Nat Struct Mol Biol 15: 764-765.
    • (2008) Nat Struct Mol Biol , vol.15 , pp. 764-765
    • Martinez-Fleites, C.1    Macauley, M.S.2    He, Y.3    Shen, D.L.4    Vocadlo, D.J.5
  • 27
    • 84870384002 scopus 로고    scopus 로고
    • O-GlcNAc transferase invokes nucleotide sugar pyrophosphate participation in catalysis
    • Schimpl M, Zheng X, Borodkin VS, Blair DE, Ferenbach AT, et al. (2012) O-GlcNAc transferase invokes nucleotide sugar pyrophosphate participation in catalysis. Nat Chem Biol 8: 969-974.
    • (2012) Nat Chem Biol , vol.8 , pp. 969-974
    • Schimpl, M.1    Zheng, X.2    Borodkin, V.S.3    Blair, D.E.4    Ferenbach, A.T.5
  • 28
    • 84860389788 scopus 로고    scopus 로고
    • Mechanistic evidence for a front-side, SNi-type reaction in a retaining glycosyltransferase
    • Lee SS, Hong SY, Errey JC, Izumi A, Davies GJ, et al. (2011) Mechanistic evidence for a front-side, SNi-type reaction in a retaining glycosyltransferase. Nat Chem Biol 7: 631-638.
    • (2011) Nat Chem Biol , vol.7 , pp. 631-638
    • Lee, S.S.1    Hong, S.Y.2    Errey, J.C.3    Izumi, A.4    Davies, G.J.5
  • 29
    • 79851508127 scopus 로고    scopus 로고
    • 6 ′′-Azido-6 ′′-deoxy-UDP-N-acetylglucosamine as a glycosyltransferase substrate
    • Mayer A, Gloster TM, Chou WK, Vocadlo DJ, Tanner ME, (2011) 6 ′′-Azido-6 ′′-deoxy-UDP-N-acetylglucosamine as a glycosyltransferase substrate. Bioorg Med Chem Lett 21: 1199-1201.
    • (2011) Bioorg Med Chem Lett , vol.21 , pp. 1199-1201
    • Mayer, A.1    Gloster, T.M.2    Chou, W.K.3    Vocadlo, D.J.4    Tanner, M.E.5
  • 32
    • 79952747341 scopus 로고    scopus 로고
    • Metabolic cross-talk allows labeling of O-linked beta-N-acetylglucosamine-modified proteins via the N-acetylgalactosamine salvage pathway
    • Boyce M, Carrico IS, Ganguli AS, Yu SH, Hangauer MJ, et al. (2011) Metabolic cross-talk allows labeling of O-linked beta-N-acetylglucosamine-modified proteins via the N-acetylgalactosamine salvage pathway. Proc Natl Acad Sci U S A 108: 3141-3146.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 3141-3146
    • Boyce, M.1    Carrico, I.S.2    Ganguli, A.S.3    Yu, S.H.4    Hangauer, M.J.5
  • 33
  • 34
    • 84860871127 scopus 로고    scopus 로고
    • Insights into O-linked N-acetylglucosamine ([0-9]O-GlcNAc) processing and dynamics through kinetic analysis of O-GlcNAc transferase and O-GlcNAcase activity on protein substrates
    • Shen DL, Gloster TM, Yuzwa SA, Vocadlo DJ, (2012) Insights into O-linked N-acetylglucosamine ([0-9]O-GlcNAc) processing and dynamics through kinetic analysis of O-GlcNAc transferase and O-GlcNAcase activity on protein substrates. J Biol Chem 287: 15395-15408.
    • (2012) J Biol Chem , vol.287 , pp. 15395-15408
    • Shen, D.L.1    Gloster, T.M.2    Yuzwa, S.A.3    Vocadlo, D.J.4
  • 35
    • 33646900710 scopus 로고    scopus 로고
    • O-linked N-acetylglucosamine proteomics of postsynaptic density preparations using lectin weak affinity chromatography and mass spectrometry
    • Vosseller K, Trinidad JC, Chalkley RJ, Specht CG, Thalhammer A, et al. (2006) O-linked N-acetylglucosamine proteomics of postsynaptic density preparations using lectin weak affinity chromatography and mass spectrometry. Mol Cell Proteomics 5: 923-934.
    • (2006) Mol Cell Proteomics , vol.5 , pp. 923-934
    • Vosseller, K.1    Trinidad, J.C.2    Chalkley, R.J.3    Specht, C.G.4    Thalhammer, A.5
  • 36
    • 77951651658 scopus 로고    scopus 로고
    • Extensive crosstalk between O-GlcNAcylation and phosphorylation regulates cytokinesis
    • Wang Z, Udeshi ND, Slawson C, Compton PD, Sakabe K, et al. (2010) Extensive crosstalk between O-GlcNAcylation and phosphorylation regulates cytokinesis. Sci Signal 3: ra2.
    • (2010) Sci Signal , vol.3
    • Wang, Z.1    Udeshi, N.D.2    Slawson, C.3    Compton, P.D.4    Sakabe, K.5
  • 37
    • 27144455345 scopus 로고    scopus 로고
    • Discovery of O-GlcNAc transferase inhibitors
    • Gross BJ, Kraybill BC, Walker S, (2005) Discovery of O-GlcNAc transferase inhibitors. J Am Chem Soc 127: 14588-14589.
    • (2005) J Am Chem Soc , vol.127 , pp. 14588-14589
    • Gross, B.J.1    Kraybill, B.C.2    Walker, S.3
  • 38
    • 67449104612 scopus 로고    scopus 로고
    • A chemoenzymatic route to N-acetylglucosamine-1-phosphate analogues: substrate specificity investigations of N-acetylhexosamine 1-kinase
    • Cai L, Guan W, Kitaoka M, Shen J, Xia C, et al. (2009) A chemoenzymatic route to N-acetylglucosamine-1-phosphate analogues: substrate specificity investigations of N-acetylhexosamine 1-kinase. Chem Commun (Camb): 2944-2946.
    • (2009) Chem Commun (Camb) , pp. 2944-2946
    • Cai, L.1    Guan, W.2    Kitaoka, M.3    Shen, J.4    Xia, C.5
  • 39
    • 80052947565 scopus 로고    scopus 로고
    • One-pot three-enzyme synthesis of UDP-GlcNAc derivatives
    • Chen Y, Thon V, Li Y, Yu H, Ding L, et al. (2011) One-pot three-enzyme synthesis of UDP-GlcNAc derivatives. Chem Commun (Camb) 47: 10815-10817.
    • (2011) Chem Commun (Camb) , vol.47 , pp. 10815-10817
    • Chen, Y.1    Thon, V.2    Li, Y.3    Yu, H.4    Ding, L.5
  • 40
    • 84863129904 scopus 로고    scopus 로고
    • Efficient one-pot multienzyme synthesis of UDP-sugars using a promiscuous UDP-sugar pyrophosphorylase from Bifidobacterium longum (BLUSP)
    • Muthana MM, Qu J, Li Y, Zhang L, Yu H, et al. (2012) Efficient one-pot multienzyme synthesis of UDP-sugars using a promiscuous UDP-sugar pyrophosphorylase from Bifidobacterium longum (BLUSP). Chem Commun (Camb) 48: 2728-2730.
    • (2012) Chem Commun (Camb) , vol.48 , pp. 2728-2730
    • Muthana, M.M.1    Qu, J.2    Li, Y.3    Zhang, L.4    Yu, H.5
  • 41
    • 33746263844 scopus 로고    scopus 로고
    • Molecular docking study and development of an empirical binding free energy model for phosphodiesterase 4 inhibitors
    • Oliveira FG, Sant'Anna CM, Caffarena ER, Dardenne LE, Barreiro EJ, (2006) Molecular docking study and development of an empirical binding free energy model for phosphodiesterase 4 inhibitors. Bioorg Med Chem 14: 6001-6011.
    • (2006) Bioorg Med Chem , vol.14 , pp. 6001-6011
    • Oliveira, F.G.1    Sant'Anna, C.M.2    Caffarena, E.R.3    Dardenne, L.E.4    Barreiro, E.J.5
  • 43
    • 29244438431 scopus 로고    scopus 로고
    • Available:. Accessed 2013 Feb 28
    • DeLano WL, Sarina Bromberg (2004) PyMOL User's Guide. Available: http://pymol.sourceforge.net/newman/userman.pdf. Accessed 2013 Feb 28.
    • (2004) PyMOL User's Guide
    • DeLano, W.L.1    Bromberg, S.2


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