메뉴 건너뛰기




Volumn 470, Issue 2, 2015, Pages 255-262

A mutant O-GlcNAcase as a probe to reveal global dynamics of protein O-GlcNAcylation during Drosophila embryonic development

Author keywords

Drosophila; Embryonic development; Fluorescence polarization; O GlcNAc probe; O GlcNAcase (OGA)

Indexed keywords

ACETYLGLUCOSAMINIDASE; MUTANT PROTEIN; N ACETYLGLUCOSAMINE; PROTEOME; BACTERIAL PROTEIN; BETA N ACETYLHEXOSAMINIDASE; HEXOSAMINIDASE C; SIGNAL TRANSDUCING ADAPTOR PROTEIN; TAB1 PROTEIN, HUMAN;

EID: 84940397727     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20150610     Document Type: Article
Times cited : (40)

References (39)
  • 1
    • 79959381299 scopus 로고    scopus 로고
    • Cross talk between O-GlcNAcylation and phosphorylation: Roles in signaling, transcription, and chronic disease
    • CrossRef PubMed
    • Hart, G., 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, 825-883 CrossRef PubMed
    • (2011) Annu. Rev. Biochem. , vol.80 , pp. 825-883
    • Hart, G.1    Slawson, C.2    Ramirez-Correa, G.3    Lagerlof, O.4
  • 2
    • 84926686351 scopus 로고    scopus 로고
    • Three decades of research on O-GlcNAcylation - A major nutrient sensor that regulates signaling, transcription and cellular metabolism
    • CrossRef PubMed
    • Hart, G.W. (2014) Three decades of research on O-GlcNAcylation - a major nutrient sensor that regulates signaling, transcription and cellular metabolism. Front. Endocrinol. 5, 183 CrossRef PubMed
    • (2014) Front. Endocrinol. , vol.5 , pp. 183
    • Hart, G.W.1
  • 3
    • 84918508564 scopus 로고    scopus 로고
    • Multiple tissue-specific roles for the O-GlcNAc post-translational modification in the induction of and complications arising from type II diabetes
    • CrossRef PubMed
    • Vaidyanathan, K. and Wells, L. (2014) Multiple tissue-specific roles for the O-GlcNAc post-translational modification in the induction of and complications arising from type II diabetes. J. Biol. Chem. 289, 34466-34471 CrossRef PubMed
    • (2014) J. Biol. Chem. , vol.289 , pp. 34466-34471
    • Vaidyanathan, K.1    Wells, L.2
  • 4
    • 84918523488 scopus 로고    scopus 로고
    • Cancer metabolism and elevated O-GlcNAc in oncogenic signaling
    • CrossRef PubMed
    • Ma, Z. and Vosseller, K. (2014) Cancer metabolism and elevated O-GlcNAc in oncogenic signaling. J. Biol. Chem. 289, 34457-34465 CrossRef PubMed
    • (2014) J. Biol. Chem. , vol.289 , pp. 34457-34465
    • Ma, Z.1    Vosseller, K.2
  • 5
    • 84918575159 scopus 로고    scopus 로고
    • The emerging link between O-GlcNAc and Alzheimer disease
    • CrossRef PubMed
    • Zhu, Y., Shan, X., Yuzwa, S.A. and Vocadlo, D.J. (2014) The emerging link between O-GlcNAc and Alzheimer disease. J. Biol. Chem. 289, 34472-34481 CrossRef PubMed
    • (2014) J. Biol. Chem. , vol.289 , pp. 34472-34481
    • Zhu, Y.1    Shan, X.2    Yuzwa, S.A.3    Vocadlo, D.J.4
  • 6
    • 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
    • CrossRef PubMed
    • Shafi, R., Iyer, S.P., Ellies, L.G., O'Donnell, N., Marek, K.W., Chui, D., Hart, G.W. and Marth, J.D. (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. U.S.A. 97, 5735-5739 CrossRef PubMed
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , 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
  • 7
    • 67650076327 scopus 로고    scopus 로고
    • Essential role of the glycosyltransferase sxc/Ogt in polycomb repression
    • CrossRef PubMed
    • Gambetta, M.C., Oktaba, K. and Muller, J. (2009) Essential role of the glycosyltransferase sxc/Ogt in polycomb repression. Science 325, 93-96 CrossRef PubMed
    • (2009) Science , vol.325 , pp. 93-96
    • Gambetta, M.C.1    Oktaba, K.2    Muller, J.3
  • 8
  • 10
    • 0035800086 scopus 로고    scopus 로고
    • Reciprocity between O-GlcNAc and O-phosphate on the carboxyl terminal domain of RNA polymerase II
    • CrossRef PubMed
    • Comer, F.I. and Hart, G.W. (2001) Reciprocity between O-GlcNAc and O-phosphate on the carboxyl terminal domain of RNA polymerase II. Biochemistry 40, 7845-7852 CrossRef PubMed
    • (2001) Biochemistry , vol.40 , pp. 7845-7852
    • Comer, F.I.1    Hart, G.W.2
  • 11
    • 79955451720 scopus 로고    scopus 로고
    • O-GlcNAc-specific antibody CTD110.6 cross-reacts with N-GlcNAc2-modified proteins induced under glucose deprivation
    • CrossRef PubMed
    • Isono, T. (2011) O-GlcNAc-specific antibody CTD110.6 cross-reacts with N-GlcNAc2-modified proteins induced under glucose deprivation. PLoS One 6, e18959 CrossRef PubMed
    • (2011) PLoS One , vol.6 , pp. e18959
    • Isono, T.1
  • 12
    • 84901054361 scopus 로고    scopus 로고
    • Characterization of the specificity of O-GlcNAc reactive antibodies under conditions of starvation and stress
    • CrossRef PubMed
    • Reeves, R.A., Lee, A., Henry, R. and Zachara, N.E. (2014) Characterization of the specificity of O-GlcNAc reactive antibodies under conditions of starvation and stress. Anal. Biochem. 457, 8-18 CrossRef PubMed
    • (2014) Anal. Biochem. , vol.457 , pp. 8-18
    • Reeves, R.A.1    Lee, A.2    Henry, R.3    Zachara, N.E.4
  • 13
    • 84876492178 scopus 로고    scopus 로고
    • Requirement of decreased O-GlcNAc glycosylation of Mef2D for its recruitment to the myogenin promoter
    • CrossRef PubMed
    • Ogawa, M., Sakakibara, Y. and Kamemura, K. (2013) Requirement of decreased O-GlcNAc glycosylation of Mef2D for its recruitment to the myogenin promoter. Biochem. Biophys. Res. Commun. 433, 558-562 CrossRef PubMed
    • (2013) Biochem. Biophys. Res. Commun. , vol.433 , pp. 558-562
    • Ogawa, M.1    Sakakibara, Y.2    Kamemura, K.3
  • 14
    • 84899006820 scopus 로고    scopus 로고
    • Antibodies that detect O-linked beta-D-N-acetylglucosamine on the extracellular domain of cell surface glycoproteins
    • CrossRef PubMed
    • Tashima, Y. and Stanley, P. (2014) Antibodies that detect O-linked beta-D-N-acetylglucosamine on the extracellular domain of cell surface glycoproteins. J. Biol. Chem. 289, 11132-11142 CrossRef PubMed
    • (2014) J. Biol. Chem. , vol.289 , pp. 11132-11142
    • Tashima, Y.1    Stanley, P.2
  • 15
    • 84921790705 scopus 로고    scopus 로고
    • Impaired O-linked N-acetylglucosaminylation in the endoplasmic reticulum by mutated epidermal growth factor (EGF) domain-specific O-linked N-acetylglucosamine transferase found in adams-oliver syndrome
    • CrossRef PubMed
    • Ogawa, M., Sawaguchi, S., Kawai, T., Nadano, D., Matsuda, T., Yagi, H., Kato, K., Furukawa, K. and Okajima, T. (2015) Impaired O-linked N-acetylglucosaminylation in the endoplasmic reticulum by mutated epidermal growth factor (EGF) domain-specific O-linked N-acetylglucosamine transferase found in adams-oliver syndrome. J. Biol. Chem. 290, 2137-2149 CrossRef PubMed
    • (2015) J. Biol. Chem. , vol.290 , pp. 2137-2149
    • Ogawa, M.1    Sawaguchi, S.2    Kawai, T.3    Nadano, D.4    Matsuda, T.5    Yagi, H.6    Kato, K.7    Furukawa, K.8    Okajima, T.9
  • 16
    • 0023257987 scopus 로고
    • Monoclonal antibodies identify a group of nuclear pore complex glycoproteins
    • CrossRef PubMed
    • Snow, C.M., Senior, A. and Gerace, L. (1987) Monoclonal antibodies identify a group of nuclear pore complex glycoproteins. J. Cell Biol. 104, 1143-1156 CrossRef PubMed
    • (1987) J. Cell Biol. , vol.104 , pp. 1143-1156
    • Snow, C.M.1    Senior, A.2    Gerace, L.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
    • PubMed
    • 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 PubMed
    • (1984) J. Biol. Chem. , vol.259 , pp. 3308-3317
    • Torres, C.R.1    Hart, G.W.2
  • 18
    • 0028346557 scopus 로고
    • Detection of O-linked N-acetylglucosamine (O-GlcNAc) on cytoplasmic and nuclear proteins
    • CrossRef PubMed
    • Roquemore, E.P., Chou, T.Y. and Hart, G.W. (1994) Detection of O-linked N-acetylglucosamine (O-GlcNAc) on cytoplasmic and nuclear proteins. Methods Enzymol. 230, 443-460 CrossRef PubMed
    • (1994) Methods Enzymol. , vol.230 , pp. 443-460
    • Roquemore, E.P.1    Chou, T.Y.2    Hart, G.W.3
  • 21
    • 0037036376 scopus 로고    scopus 로고
    • Structure-based design of beta 1, 4-galactosyltransferase i (beta 4Gal-T1) with equally efficient N-acetylgalactosaminyltransferase activity: Point mutation broadens beta 4Gal-T1 donor specificity
    • CrossRef PubMed
    • Ramakrishnan, B. and Qasba, P.K. (2002) Structure-based design of beta 1, 4-galactosyltransferase I (beta 4Gal-T1) with equally efficient N-acetylgalactosaminyltransferase activity: point mutation broadens beta 4Gal-T1 donor specificity. J. Biol. Chem. 277, 20833-20839 CrossRef PubMed
    • (2002) J. Biol. Chem. , vol.277 , pp. 20833-20839
    • Ramakrishnan, B.1    Qasba, P.K.2
  • 23
    • 33645735070 scopus 로고    scopus 로고
    • Structural insights into the mechanism and inhibition of eukaryotic O-GlcNAc hydrolysis
    • CrossRef PubMed
    • Rao, F.V., Dorfmueller, H.C., Villa, F., Allwood, M., Eggleston, I.M. and van Aalten, D.M. (2006) Structural insights into the mechanism and inhibition of eukaryotic O-GlcNAc hydrolysis. EMBO J. 25, 1569-1578 CrossRef PubMed
    • (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
  • 24
    • 33845944034 scopus 로고    scopus 로고
    • GlcNAcstatin: A picomolar, selective O-GlcNAcase inhibitor that modulates intracellular O-glcNAcylation levels
    • CrossRef PubMed
    • Dorfmueller, H.C., Borodkin, V.S., Schimpl, M., Shepherd, S.M., Shpiro, N.A. and van Aalten, D.M. (2006) GlcNAcstatin: a picomolar, selective O-GlcNAcase inhibitor that modulates intracellular O-glcNAcylation levels. J. Am. Chem. Soc. 128, 16484-16485 CrossRef PubMed
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 16484-16485
    • Dorfmueller, H.C.1    Borodkin, V.S.2    Schimpl, M.3    Shepherd, S.M.4    Shpiro, N.A.5    Van Aalten, D.M.6
  • 25
    • 84857548992 scopus 로고    scopus 로고
    • Synergy of peptide and sugar in O-GlcNAcase substrate recognition
    • CrossRef PubMed
    • Schimpl, M., Borodkin, V.S., Gray, L.J. and van Aalten, D.M. (2012) Synergy of peptide and sugar in O-GlcNAcase substrate recognition. Chem. Biol. 19, 173-178 CrossRef PubMed
    • (2012) Chem. Biol. , vol.19 , pp. 173-178
    • Schimpl, M.1    Borodkin, V.S.2    Gray, L.J.3    Van Aalten, D.M.4
  • 27
    • 66549119673 scopus 로고    scopus 로고
    • GlcNAcstatins are nanomolar inhibitors of human O-GlcNAcase inducing cellular hyper-O-GlcNAcylation
    • CrossRef PubMed
    • Dorfmueller, H.C., Borodkin, V.S., Schimpl, M. and van Aalten, D.M. (2009) GlcNAcstatins are nanomolar inhibitors of human O-GlcNAcase inducing cellular hyper-O-GlcNAcylation. Biochem. J. 420, 221-227 CrossRef PubMed
    • (2009) Biochem. J. , vol.420 , pp. 221-227
    • Dorfmueller, H.C.1    Borodkin, V.S.2    Schimpl, M.3    Van Aalten, D.M.4
  • 28
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • CrossRef PubMed
    • Emsley, P. and Cowtan, K. (2004) Coot: model-building tools for molecular graphics. Acta. Crystallogr. D Biol. Crystallogr. 60, 2126-2132 CrossRef PubMed
    • (2004) Acta. Crystallogr. D Biol. Crystallogr. , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 29
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • CrossRef PubMed
    • Murshudov, G.N., Vagin, A.A. and Dodson, E.J. (1997) Refinement of macromolecular structures by the maximum-likelihood method. Acta. Crystallogr. D Biol. Crystallogr. 53, 240-255 CrossRef PubMed
    • (1997) Acta. Crystallogr. D Biol. Crystallogr. , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 31
    • 13844313884 scopus 로고    scopus 로고
    • Proteomic analysis of the wing imaginal discs of Drosophila melanogaster
    • CrossRef PubMed
    • Alonso, J. and Santaren, J.F. (2005) Proteomic analysis of the wing imaginal discs of Drosophila melanogaster . Proteomics 5, 474-489 CrossRef PubMed
    • (2005) Proteomics , vol.5 , pp. 474-489
    • Alonso, J.1    Santaren, J.F.2
  • 33
    • 84864088377 scopus 로고    scopus 로고
    • Role of host cell factor-1 in cell cycle regulation
    • CrossRef PubMed
    • Zargar, Z. and Tyagi, S. (2012) Role of host cell factor-1 in cell cycle regulation. Transcription 3, 187-192 CrossRef PubMed
    • (2012) Transcription , vol.3 , pp. 187-192
    • Zargar, Z.1    Tyagi, S.2
  • 37
    • 52049120841 scopus 로고    scopus 로고
    • Regulation of the O-linked beta-N-acetylglucosamine transferase by insulin signaling
    • CrossRef PubMed
    • Whelan, S.A., Lane, M.D. and Hart, G.W. (2008) Regulation of the O-linked beta-N-acetylglucosamine transferase by insulin signaling. J. Biol. Chem. 283, 21411-21417 CrossRef PubMed
    • (2008) J. Biol. Chem. , vol.283 , pp. 21411-21417
    • Whelan, S.A.1    Lane, M.D.2    Hart, G.W.3
  • 38
    • 62449289296 scopus 로고    scopus 로고
    • Survey of O-GlcNAc level variations in Xenopus laevis from oogenesis to early development
    • CrossRef PubMed
    • Dehennaut, V., Lefebvre, T., Leroy, Y., Vilain, J.P., Michalski, J.C. and Bodart, J.F. (2009) Survey of O-GlcNAc level variations in Xenopus laevis from oogenesis to early development. Glycoconj. J. 26, 301-311 CrossRef PubMed
    • (2009) Glycoconj. J. , vol.26 , pp. 301-311
    • Dehennaut, V.1    Lefebvre, T.2    Leroy, Y.3    Vilain, J.P.4    Michalski, J.C.5    Bodart, J.F.6
  • 39
    • 84918582083 scopus 로고    scopus 로고
    • O-GlcNAcylation prevents aggregation of the polycomb group repressor polyhomeotic
    • CrossRef PubMed
    • Gambetta, M.C. and Muller, J. (2014) O-GlcNAcylation prevents aggregation of the polycomb group repressor polyhomeotic. Dev. Cell 31, 629-639 CrossRef PubMed
    • (2014) Dev. Cell , vol.31 , pp. 629-639
    • Gambetta, M.C.1    Muller, J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.