메뉴 건너뛰기




Volumn 5, Issue 12, 2015, Pages

Dual functionality of O-GlcNAc transferase is required for Drosophila development

Author keywords

Drosophila development; Hox; O GlcNAc; O GlcNAc transferase

Indexed keywords

DROSOPHILA PROTEIN; N ACETYLGLUCOSAMINYLTRANSFERASE; O-GLCNAC TRANSFERASE;

EID: 84962310803     PISSN: None     EISSN: 20462441     Source Type: Journal    
DOI: 10.1098/rsob.150234     Document Type: Article
Times cited : (26)

References (48)
  • 1
    • 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. (doi:10.1038/nature05815)
    • (2007) Nature , vol.446 , pp. 1017-1022
    • Hart, G.W.1    Housley, M.P.2    Slawson, C.3
  • 2
    • 79959381299 scopus 로고    scopus 로고
    • Cross talk between O-GlcNaCylation and phosphorylation: Roles in signaling, transcription, and chronic disease
    • Hart G, 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, 825-883. (doi:10.1146/annurev-biochem-060608-102511)
    • (2011) Annu. Rev. Biochem. , vol.80 , pp. 825-883
    • Hart, G.1    Slawson, C.2    Ramirez-Correa, G.3    Lagerlof, O.4
  • 3
    • 84355161950 scopus 로고    scopus 로고
    • GlcNAcylation of histone H2B facilitates its monoubiquitination
    • Fujiki R et al. 2011 GlcNAcylation of histone H2B facilitates its monoubiquitination. Nature 480, 557-560. (doi:10.1038/nature10656)
    • (2011) Nature , vol.480 , pp. 557-560
    • Fujiki, R.1
  • 5
    • 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. (doi:10.1038/nature09638)
    • (2011) Nature , vol.469 , pp. 564-567
    • Lazarus, M.B.1    Nam, Y.2    Jiang, J.3    Sliz, P.4    Walker, S.5
  • 6
    • 84870384002 scopus 로고    scopus 로고
    • O-GlcNaC transferase invokes nucleotide sugar pyrophosphate participation in catalysis
    • Schimpl M et al. 2012 O-GlcNAc transferase invokes nucleotide sugar pyrophosphate participation in catalysis. Nat. Chem. Biol. 8, 969-974. (doi:10.1038/nchembio.1108)
    • (2012) Nat. Chem. Biol. , vol.8 , pp. 969-974
    • Schimpl, M.1
  • 7
    • 84857933257 scopus 로고    scopus 로고
    • Structural and functional discussion of the tetra-trico-peptide repeat, a protein interaction module
    • Zeytuni N, Zarivach R. 2012 Structural and functional discussion of the tetra-trico-peptide repeat, a protein interaction module. Structure 20, 397-405. (doi:10.1016/j.str.2012.01.006)
    • (2012) Structure , vol.20 , pp. 397-405
    • Zeytuni, N.1    Zarivach, R.2
  • 8
    • 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, Conti E. 2004 The superhelical TPR-repeat domain of O-linked GlcNAc transferase exhibits structural similarities to importin alpha. Nat. Struct. Mol. Biol. 11, 1001-1007. (doi:10.1038/nsmb833)
    • (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    Conti, E.6
  • 9
    • 0037648473 scopus 로고    scopus 로고
    • Identification and cloning of a novel family of coiled-coil domain proteins that interact with O-GlcNAc transferase
    • Iyer SP, Akimoto Y, Hart GW 2003 Identification and cloning of a novel family of coiled-coil domain proteins that interact with O-GlcNAc transferase. J. Biol. Chem. 278, 5399-5409. (doi:10.1074/jbc.M209384200)
    • (2003) J. Biol. Chem. , vol.278 , pp. 5399-5409
    • Iyer, S.P.1    Akimoto, Y.2    Hart, G.W.3
  • 10
    • 0037067659 scopus 로고    scopus 로고
    • Recruitment of O-GlcNaC transferase to promoters by corepressor mSin3A: Coupling protein O-GlcNaCylation to transcriptional repression
    • Yang X, Zhang F, Kudlow JE 2002 Recruitment of O-GlcNAc transferase to promoters by corepressor mSin3A: coupling protein O-GlcNAcylation to transcriptional repression. Cell 110, 69-80. (doi:10.1016/S0092-8674(02)00810-3)
    • (2002) Cell , vol.110 , pp. 69-80
    • Yang, X.1    Zhang, F.2    Kudlow, J.E.3
  • 11
    • 84872953223 scopus 로고    scopus 로고
    • TET2 promotes histone O-GlcNaCylation during gene transcription
    • Chen Q, Chen Y, Bian C, Fujiki R, Yu X. 2013 TET2 promotes histone O-GlcNAcylation during gene transcription. Nature 493, 561-564. (doi:10.1038/nature11742)
    • (2013) Nature , vol.493 , pp. 561-564
    • Chen, Q.1    Chen, Y.2    Bian, C.3    Fujiki, R.4    Yu, X.5
  • 12
    • 45149095784 scopus 로고    scopus 로고
    • AMP-activated protein kinase and p38 MAPK activate O-GlcNaCylation of neuronal proteins during glucose deprivation
    • Cheung WD, Hart GW 2008 AMP-activated protein kinase and p38 MAPK activate O-GlcNAcylation of neuronal proteins during glucose deprivation. J. Biol. Chem. 283, 13009-13020. (doi:10.1074/jbc.M801222200)
    • (2008) J. Biol. Chem. , vol.283 , pp. 13009-13020
    • Cheung, W.D.1    Hart, G.W.2
  • 13
    • 33646159532 scopus 로고    scopus 로고
    • Recombinant O-GlcNAc transferase isoforms: Identification of O-GlcNaCase, yes tyrosine kinase, and tau as isoform-specific substrates
    • Lazarus BD, Love DC, Hanover JA 2006 Recombinant O-GlcNAc transferase isoforms: identification of O-GlcNAcase, yes tyrosine kinase, and tau as isoform-specific substrates. Glycobiology 16, 415-421. (doi:10.1093/glycob/cwj078)
    • (2006) Glycobiology , vol.16 , pp. 415-421
    • Lazarus, B.D.1    Love, D.C.2    Hanover, J.A.3
  • 14
    • 0042090275 scopus 로고    scopus 로고
    • Roles of the tetratricopeptide repeat domain in O-GlcNAc transferase targeting and protein substrate specificity
    • Iyer SP, Hart GW 2003 Roles of the tetratricopeptide repeat domain in O-GlcNAc transferase targeting and protein substrate specificity. J. Biol. Chem. 278, 24608-24616. (doi:10.1074/jbc.M300036200)
    • (2003) J. Biol. Chem. , vol.278 , pp. 24608-24616
    • Iyer, S.P.1    Hart, G.W.2
  • 15
    • 25844440804 scopus 로고    scopus 로고
    • Transcriptional regulation and O-GlcNaCylation activity of zebrafish OGT during embryogenesis
    • Sohn KC, Do SI 2005 Transcriptional regulation and O-GlcNAcylation activity of zebrafish OGT during embryogenesis. Biochem. Biophys. Res. Commun. 337, 256-263. (doi:10.1016/j.bbrc.2005.09.049)
    • (2005) Biochem. Biophys. Res. Commun. , vol.337 , pp. 256-263
    • Sohn, K.C.1    Do, S.I.2
  • 16
    • 0034705030 scopus 로고    scopus 로고
    • The O-GlcNAc transferase gene resides on the X chromosome and is essential for embryonic stem cell viability and mouse ontogeny
    • Shafi R, Iyer SP, Ellies LG, O'Donnell N, Marek KW, Chui D, Hart GW, Marth JD 2000 The O-GlcNAc transferase gene resides on the X chromosome and is essential for embryonic stem cell viability and mouse ontogeny. Proc. Natl Acad. Sci. USA 97, 5735-5739. (doi:10.1073/pnas.100471497)
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 5735-5739
    • Shafi, R.1    Iyer, S.P.2    Ellies, L.G.3    O'Donnell, N.4    Marek, K.W.5    Chui, D.6    Hart, G.W.7    Marth, J.D.8
  • 17
    • 0842347416 scopus 로고    scopus 로고
    • Ogt-dependent X-chromosome-linked protein glycosylation is a requisite modification in somatic cell function and embryo viability
    • O'Donnell N, Zachara NE, Hart GW, Marth JD 2004 Ogt-dependent X-chromosome-linked protein glycosylation is a requisite modification in somatic cell function and embryo viability. Mol. Cell Biol. 24, 1680-1690. (doi:10.1128/MCB.24.4.1680-1690.2004)
    • (2004) Mol. Cell Biol. , vol.24 , pp. 1680-1690
    • O'Donnell, N.1    Zachara, N.E.2    Hart, G.W.3    Marth, J.D.4
  • 18
    • 0942276434 scopus 로고    scopus 로고
    • Pilot morpholino screen in xenopus tropicalis identifies a novel gene involved in head development
    • Kenwrick S, Amaya E, Papalopulu N. 2004 Pilot morpholino screen in Xenopus tropicalis identifies a novel gene involved in head development. Dev Dyn. 229, 289-299. (doi:10.1002/dvdy.10440)
    • (2004) Dev Dyn. , vol.229 , pp. 289-299
    • Kenwrick, S.1    Amaya, E.2    Papalopulu, N.3
  • 20
    • 67650076327 scopus 로고    scopus 로고
    • Essential role of the glycosyltransferase sxc/Ogt in polycomb repression
    • Gambetta MC, Oktaba K, Muller J. 2009 Essential role of the glycosyltransferase sxc/Ogt in polycomb repression. Science 325, 93-96. (doi:10.1126/science.1169727)
    • (2009) Science , vol.325 , pp. 93-96
    • Gambetta, M.C.1    Oktaba, K.2    Muller, J.3
  • 21
    • 0021670304 scopus 로고
    • A gene that regulates the bithorax complex differentially in larval and adult cells of drosophila
    • Ingham PW. 1984 A gene that regulates the bithorax complex differentially in larval and adult cells of Drosophila. Cell 37, 815-823. (doi:10.1016/0092-8674(84)90416-1)
    • (1984) Cell , vol.37 , pp. 815-823
    • Ingham, P.W.1
  • 23
    • 23844481789 scopus 로고    scopus 로고
    • A caenorhabditis elegans model of insulin resistance: Altered macronutrient storage and dauer formation in an OGT-1 knockout
    • Hanover JA, Forsythe ME, Hennessey PT, Brodigan TM, Love DC, Ashwell G, Krause M. 2005 A Caenorhabditis elegans model of insulin resistance: altered macronutrient storage and dauer formation in an OGT-1 knockout. Proc. Natl Acad. Sci. USA 102, 11266-11271. (doi:10.1073/pnas.0408771102)
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 11266-11271
    • Hanover, J.A.1    Forsythe, M.E.2    Hennessey, P.T.3    Brodigan, T.M.4    Love, D.C.5    Ashwell, G.6    Krause, M.7
  • 24
    • 33644922089 scopus 로고    scopus 로고
    • SECRET AGENT and SPINDLY have overlapping roles in the development of arabidopsis thaliana L
    • Hartweck LM, Genger RK, Grey WM, Olszewski NE 2006 SECRET AGENT and SPINDLY have overlapping roles in the development of Arabidopsis thaliana L. Heyn. J. Exp. Bot. 57, 865-875. (doi:10.1093/jxb/erj071)
    • (2006) Heyn. J. Exp. Bot. , vol.57 , pp. 865-875
    • Hartweck, L.M.1    Genger, R.K.2    Grey, W.M.3    Olszewski, N.E.4
  • 26
    • 84868031059 scopus 로고    scopus 로고
    • Understanding the targeting of the RB family proteins by viral oncoproteins to defeat their oncogenic machinery
    • Bellacchio E, Paggi MG 2013 Understanding the targeting of the RB family proteins by viral oncoproteins to defeat their oncogenic machinery. J. Cell Physiol. 228, 285-291. (doi:10.1002/jcp.24137)
    • (2013) J. Cell Physiol. , vol.228 , pp. 285-291
    • Bellacchio, E.1    Paggi, M.G.2
  • 30
    • 33645735070 scopus 로고    scopus 로고
    • Structural insights into the mechanism and inhibition of eukaryotic O-GlcNaC hydrolysis
    • Rao FV, Dorfmueller HC, Villa F, Allwood M, Eggleston IM, van Aalten DM. 2006 Structural insights into the mechanism and inhibition of eukaryotic O-GlcNAc hydrolysis. EMBO J. 25, 1569-1578. (doi:10.1038/sj.emboj.7601026)
    • (2006) EMBO J. , vol.25 , pp. 1569-1578
    • Rao, F.V.1    Dorfmueller, H.C.2    Villa, F.3    Allwood, M.4    Eggleston, I.M.5    Van Aalten, D.M.6
  • 32
    • 84918582083 scopus 로고    scopus 로고
    • O-GlcNaCylation prevents aggregation of the polycomb group repressor polyhomeotic
    • Gambetta MC, Muller J. 2014 O-GlcNAcylation prevents aggregation of the polycomb group repressor polyhomeotic. Dev. Cell. 31, 629-639. (doi:10.1016/j.devcel.2014.10.020)
    • (2014) Dev. Cell. , vol.31 , pp. 629-639
    • Gambetta, M.C.1    Muller, J.2
  • 33
    • 39749104251 scopus 로고    scopus 로고
    • Phosphoinositide signalling links O-GlcNaC transferase to insulin resistance
    • Yang X et al. 2008 Phosphoinositide signalling links O-GlcNAc transferase to insulin resistance. Nature 451, 964-969. (doi:10.1038/nature06668)
    • (2008) Nature , vol.451 , pp. 964-969
    • Yang, X.1
  • 34
    • 0034948273 scopus 로고    scopus 로고
    • Ectopic expression of the tetratricopeptide repeat domain of SPINDLY causes defects in gibberellin response
    • Tseng TS, Swain SM, Olszewski NE 2001 Ectopic expression of the tetratricopeptide repeat domain of SPINDLY causes defects in gibberellin response. Plant Physiol. 126, 1250-1258. (doi:10.1104/pp.126.3.1250)
    • (2001) Plant Physiol. , vol.126 , pp. 1250-1258
    • Tseng, T.S.1    Swain, S.M.2    Olszewski, N.E.3
  • 35
    • 84906493054 scopus 로고    scopus 로고
    • Molecular architecture and mechanism of the anaphase-promoting complex
    • Chang L, Zhang Z, Yang J, McLaughlin SH, Barford D. 2014 Molecular architecture and mechanism of the anaphase-promoting complex. Nature 513, 388-393. (doi:10.1038/nature13543)
    • (2014) Nature , vol.513 , pp. 388-393
    • Chang, L.1    Zhang, Z.2    Yang, J.3    McLaughlin, S.H.4    Barford, D.5
  • 36
    • 84902125445 scopus 로고    scopus 로고
    • TMTC1 and TMTC2 are novel endoplasmic reticulum tetratricopeptide repeat-containing adapter proteins involved in calcium homeostasis
    • Sunryd JC, Cheon B, Graham JB, Giorda KM, Fissore RA, Hebert DN 2014 TMTC1 and TMTC2 are novel endoplasmic reticulum tetratricopeptide repeat-containing adapter proteins involved in calcium homeostasis. J. Biol. Chem. 289, 16085-16099. (doi:10.1074/jbc.M114.554071)
    • (2014) J. Biol. Chem. , vol.289 , pp. 16085-16099
    • Sunryd, J.C.1    Cheon, B.2    Graham, J.B.3    Giorda, K.M.4    Fissore, R.A.5    Hebert, D.N.6
  • 37
    • 0034646511 scopus 로고    scopus 로고
    • Structure of TPR domain-peptide complexes: Critical elements in the assembly of the hsp70-hsp90 multichaperone machine
    • Scheufler C, Brinker A, Bourenkov G, Pegoraro S, Moroder L, Bartunik H, Hartl FU, Moarefi I. 2000 Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine. Cell 101, 199-210. (doi:10.1016/S0092-8674(00)80830-2)
    • (2000) Cell , vol.101 , pp. 199-210
    • Scheufler, C.1    Brinker, A.2    Bourenkov, G.3    Pegoraro, S.4    Moroder, L.5    Bartunik, H.6    Hartl, F.U.7    Moarefi, I.8
  • 38
    • 33745841363 scopus 로고    scopus 로고
    • Crystal structure of yeast mitochondrial outer membrane translocon member tom70p
    • Wu Y, Sha B. 2006 Crystal structure of yeast mitochondrial outer membrane translocon member Tom70p. Nat. Struct. Mol. Biol. 13, 589-593. (doi:10.1038/nsmb1106)
    • (2006) Nat. Struct. Mol. Biol. , vol.13 , pp. 589-593
    • Wu, Y.1    Sha, B.2
  • 41
    • 82955214036 scopus 로고    scopus 로고
    • Drosophila melanogaster dHCF interacts with both PcG and TrxG epigenetic regulators
    • Rodriguez-Jato S, Busturia A, Herr W. 2011 Drosophila melanogaster dHCF interacts with both PcG and TrxG epigenetic regulators. PLoS ONE 6, e27479. (doi:10.1371/journal.pone.0027479)
    • (2011) PLoS ONE , vol.6
    • Rodriguez-Jato, S.1    Busturia, A.2    Herr, W.3
  • 42
    • 79959334683 scopus 로고    scopus 로고
    • Polycomb repressive complex 2 is necessary for the normal site-specific O-GlcNaC distribution in mouse embryonic stem cells
    • Myers SA, Panning B, Burlingame AL 2011 Polycomb repressive complex 2 is necessary for the normal site-specific O-GlcNAc distribution in mouse embryonic stem cells. Proc. Natl Acad. Sci. USA 108, 9490-9495. (doi:10.1073/pnas.1019289108)
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 9490-9495
    • Myers, S.A.1    Panning, B.2    Burlingame, A.L.3
  • 44
    • 0037853130 scopus 로고    scopus 로고
    • YY1 is regulated by O-linked N-acetylglucosaminylation (O-GlcNAcylation)
    • Hiromura M, Choi CH, Sabourin NA, Jones H, Bachvarov D, Usheva A. 2003 YY1 is regulated by O-linked N-acetylglucosaminylation (O-GlcNAcylation). J. Biol. Chem. 278, 14046-14052. (doi:10.1074/jbc.M300789200)
    • (2003) J. Biol. Chem. , vol.278 , pp. 14046-14052
    • Hiromura, M.1    Choi, C.H.2    Sabourin, N.A.3    Jones, H.4    Bachvarov, D.5    Usheva, A.6
  • 45
    • 0000560808 scopus 로고    scopus 로고
    • MOLREP: An automated program for molecular replacement
    • Vagin A, Teplyakov A. 1997 MOLREP: an automated program for molecular replacement. J. Appl. Crystallogr. 30, 1022-1025. (doi:10.1107/S0021889897006766)
    • (1997) J. Appl. Crystallogr. , vol.30 , pp. 1022-1025
    • Vagin, A.1    Teplyakov, A.2
  • 46
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • Emsley P, Cowtan K. 2004 Coot: model-building tools for molecular graphics. Acta Crystallogr. D, Biol. Crystallogr. 60, 2126-2132. (doi:10.1107/S0907444904019158)
    • (2004) Acta Crystallogr. D, Biol. Crystallogr. , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 47
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov GN, Vagin AA, Dodson EJ 1997 Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr. D, Biol. Crystallogr. 53, 240-255. (doi:10.1107/S0907444996012255)
    • (1997) Acta Crystallogr. D, Biol. Crystallogr. , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 48
    • 49649091094 scopus 로고    scopus 로고
    • Immunolabeling of embryos
    • Muller HA. 2008 Immunolabeling of embryos. Methods Mol Biol. 420, 207-218. (doi:10.1007/978-1-59745-583-1-12)
    • (2008) Methods Mol Biol. , vol.420 , pp. 207-218
    • Muller, H.A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.