메뉴 건너뛰기




Volumn 22, Issue 4, 2014, Pages 590-601

Structural basis of substrate specificity of human oligosaccharyl transferase subunit N33/Tusc3 and its role in regulating protein N-glycosylation

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE; OLIGOSACCHARIDE; OLIGOSACCHARYLTRANSFERASE SUBUNIT N33; THIOREDOXIN; TRANSFERASE; UNCLASSIFIED DRUG; GLUTATHIONE; OLIGOSACCHARYL TRANSFERASE SUBUNIT N33; OLIGOSACCHARYL TRANSFERASE SUBUNIT TUSC3; PEPTIDE FRAGMENT; DISULFIDE; MEMBRANE PROTEIN; N33 PROTEIN, HUMAN; PEPTIDE; PROTEIN BINDING; PROTEIN SUBUNIT; RECOMBINANT PROTEIN; TUMOR SUPPRESSOR PROTEIN;

EID: 84898469110     PISSN: 09692126     EISSN: 18784186     Source Type: Journal    
DOI: 10.1016/j.str.2014.02.013     Document Type: Article
Times cited : (74)

References (47)
  • 3
    • 80052796983 scopus 로고    scopus 로고
    • Reactivity of thioredoxin as a protein thiol-disulfide oxidoreductase
    • Z. Cheng, J. Zhang, D.P. Ballou, and C.H. Williams Jr. Reactivity of thioredoxin as a protein thiol-disulfide oxidoreductase Chem. Rev. 111 2011 5768 5783
    • (2011) Chem. Rev. , vol.111 , pp. 5768-5783
    • Cheng, Z.1    Zhang, J.2    Ballou, D.P.3    Williams, Jr.C.H.4
  • 6
    • 0033135747 scopus 로고    scopus 로고
    • Protein glycosylation in development and disease
    • J.W. Dennis, M. Granovsky, and C.E. Warren Protein glycosylation in development and disease Bioessays 21 1999 412 421
    • (1999) Bioessays , vol.21 , pp. 412-421
    • Dennis, J.W.1    Granovsky, M.2    Warren, C.E.3
  • 7
    • 0030219388 scopus 로고    scopus 로고
    • Why mammalian cell surface proteins are glycoproteins
    • C.G. Gahmberg, and M. Tolvanen Why mammalian cell surface proteins are glycoproteins Trends Biochem. Sci. 21 1996 308 311
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 308-311
    • Gahmberg, C.G.1    Tolvanen, M.2
  • 10
    • 79958200530 scopus 로고    scopus 로고
    • Solution structure of a human minimembrane protein Ost4, a subunit of the oligosaccharyltransferase complex
    • S. Gayen, and C. Kang Solution structure of a human minimembrane protein Ost4, a subunit of the oligosaccharyltransferase complex Biochem. Biophys. Res. Commun. 409 2011 572 576
    • (2011) Biochem. Biophys. Res. Commun. , vol.409 , pp. 572-576
    • Gayen, S.1    Kang, C.2
  • 12
    • 0028198111 scopus 로고
    • How N-linked oligosaccharides affect glycoprotein folding in the endoplasmic reticulum
    • A. Helenius How N-linked oligosaccharides affect glycoprotein folding in the endoplasmic reticulum Mol. Biol. Cell 5 1994 253 265
    • (1994) Mol. Biol. Cell , vol.5 , pp. 253-265
    • Helenius, A.1
  • 13
    • 3943059566 scopus 로고    scopus 로고
    • Roles of N-linked glycans in the endoplasmic reticulum
    • A. Helenius, and M. Aebi Roles of N-linked glycans in the endoplasmic reticulum Annu. Rev. Biochem. 73 2004 1019 1049
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 1019-1049
    • Helenius, A.1    Aebi, M.2
  • 14
    • 0025832056 scopus 로고
    • Translational control in mammalian cells
    • J.W.B. Hershey Translational control in mammalian cells Annu. Rev. Biochem. 60 1991 717 755
    • (1991) Annu. Rev. Biochem. , vol.60 , pp. 717-755
    • Hershey, J.W.B.1
  • 15
    • 84866551625 scopus 로고    scopus 로고
    • Eukaryotic N-glycosylation occurs via the membrane-anchored C-terminal domain of the Stt3p subunit of oligosaccharyltransferase
    • C. Huang, R. Bhaskaran, and S. Mohanty Eukaryotic N-glycosylation occurs via the membrane-anchored C-terminal domain of the Stt3p subunit of oligosaccharyltransferase J. Biol. Chem. 287 2012 32450 32458
    • (2012) J. Biol. Chem. , vol.287 , pp. 32450-32458
    • Huang, C.1    Bhaskaran, R.2    Mohanty, S.3
  • 16
    • 0026698060 scopus 로고
    • Oxidized redox state of glutathione in the endoplasmic reticulum
    • C. Hwang, A.J. Sinskey, and H.F. Lodish Oxidized redox state of glutathione in the endoplasmic reticulum Science 257 1992 1496 1502
    • (1992) Science , vol.257 , pp. 1496-1502
    • Hwang, C.1    Sinskey, A.J.2    Lodish, H.F.3
  • 17
    • 79954479197 scopus 로고    scopus 로고
    • Polypeptide binding specificities of Saccharomyces cerevisiae oligosaccharyltransferase accessory proteins Ost3p and Ost6p
    • M.F. Jamaluddin, U.M. Bailey, N.Y. Tan, A.P. Stark, and B.L. Schulz Polypeptide binding specificities of Saccharomyces cerevisiae oligosaccharyltransferase accessory proteins Ost3p and Ost6p Protein Sci. 20 2011 849 855
    • (2011) Protein Sci. , vol.20 , pp. 849-855
    • Jamaluddin, M.F.1    Bailey, U.M.2    Tan, N.Y.3    Stark, A.P.4    Schulz, B.L.5
  • 18
    • 33645103490 scopus 로고    scopus 로고
    • An evolving view of the eukaryotic oligosaccharyltransferase
    • D.J. Kelleher, and R. Gilmore An evolving view of the eukaryotic oligosaccharyltransferase Glycobiology 16 2006 47R 62R
    • (2006) Glycobiology , vol.16
    • Kelleher, D.J.1    Gilmore, R.2
  • 19
    • 0038294237 scopus 로고    scopus 로고
    • Oligosaccharyltransferase isoforms that contain different catalytic STT3 subunits have distinct enzymatic properties
    • D.J. Kelleher, D. Karaoglu, E.C. Mandon, and R. Gilmore Oligosaccharyltransferase isoforms that contain different catalytic STT3 subunits have distinct enzymatic properties Mol. Cell 12 2003 101 111
    • (2003) Mol. Cell , vol.12 , pp. 101-111
    • Kelleher, D.J.1    Karaoglu, D.2    Mandon, E.C.3    Gilmore, R.4
  • 23
    • 79959191882 scopus 로고    scopus 로고
    • X-ray structure of a bacterial oligosaccharyltransferase
    • C. Lizak, S. Gerber, S. Numao, M. Aebi, and K.P. Locher X-ray structure of a bacterial oligosaccharyltransferase Nature 474 2011 350 355
    • (2011) Nature , vol.474 , pp. 350-355
    • Lizak, C.1    Gerber, S.2    Numao, S.3    Aebi, M.4    Locher, K.P.5
  • 24
    • 0030201104 scopus 로고    scopus 로고
    • Structure and methylation-associated silencing of a gene within a homozygously deleted region of human chromosome band 8p22
    • D. MacGrogan, A. Levy, G.S. Bova, W.B. Isaacs, and R. Bookstein Structure and methylation-associated silencing of a gene within a homozygously deleted region of human chromosome band 8p22 Genomics 35 1996 55 65
    • (1996) Genomics , vol.35 , pp. 55-65
    • Macgrogan, D.1    Levy, A.2    Bova, G.S.3    Isaacs, W.B.4    Bookstein, R.5
  • 25
    • 79961171901 scopus 로고    scopus 로고
    • Oligosaccharyltransferase: The central enzyme of N-linked protein glycosylation
    • E. Mohorko, R. Glockshuber, and M. Aebi Oligosaccharyltransferase: the central enzyme of N-linked protein glycosylation J. Inherit. Metab. Dis. 34 2011 869 878
    • (2011) J. Inherit. Metab. Dis. , vol.34 , pp. 869-878
    • Mohorko, E.1    Glockshuber, R.2    Aebi, M.3
  • 27
    • 0034623005 scopus 로고    scopus 로고
    • T-Coffee: A novel method for fast and accurate multiple sequence alignment
    • C. Notredame, D.G. Higgins, and J. Heringa T-Coffee: A novel method for fast and accurate multiple sequence alignment J. Mol. Biol. 302 2000 205 217
    • (2000) J. Mol. Biol. , vol.302 , pp. 205-217
    • Notredame, C.1    Higgins, D.G.2    Heringa, J.3
  • 28
    • 33748195979 scopus 로고    scopus 로고
    • Glycosylation in cellular mechanisms of health and disease
    • K. Ohtsubo, and J.D. Marth Glycosylation in cellular mechanisms of health and disease Cell 126 2006 855 867
    • (2006) Cell , vol.126 , pp. 855-867
    • Ohtsubo, K.1    Marth, J.D.2
  • 29
    • 1342327544 scopus 로고    scopus 로고
    • Statistical analysis of the protein environment of N-glycosylation sites: Implications for occupancy, structure, and folding
    • A.J. Petrescu, A.L. Milac, S.M. Petrescu, R.A. Dwek, and M.R. Wormald Statistical analysis of the protein environment of N-glycosylation sites: implications for occupancy, structure, and folding Glycobiology 14 2004 103 114
    • (2004) Glycobiology , vol.14 , pp. 103-114
    • Petrescu, A.J.1    Milac, A.L.2    Petrescu, S.M.3    Dwek, R.A.4    Wormald, M.R.5
  • 31
    • 0026781216 scopus 로고
    • Equilibrium and kinetic constants for the thiol-disulfide interchange reaction between glutathione and dithiothreitol
    • D.M. Rothwarf, and H.A. Scheraga Equilibrium and kinetic constants for the thiol-disulfide interchange reaction between glutathione and dithiothreitol Proc. Natl. Acad. Sci. USA 89 1992 7944 7948
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 7944-7948
    • Rothwarf, D.M.1    Scheraga, H.A.2
  • 32
    • 58249093866 scopus 로고    scopus 로고
    • Cotranslational and posttranslational N-glycosylation of polypeptides by distinct mammalian OST isoforms
    • C. Ruiz-Canada, D.J. Kelleher, and R. Gilmore Cotranslational and posttranslational N-glycosylation of polypeptides by distinct mammalian OST isoforms Cell 136 2009 272 283
    • (2009) Cell , vol.136 , pp. 272-283
    • Ruiz-Canada, C.1    Kelleher, D.J.2    Gilmore, R.3
  • 33
    • 61649089751 scopus 로고    scopus 로고
    • Analysis of glycosylation site occupancy reveals a role for Ost3p and Ost6p in site-specific N-glycosylation efficiency
    • B.L. Schulz, and M. Aebi Analysis of glycosylation site occupancy reveals a role for Ost3p and Ost6p in site-specific N-glycosylation efficiency Mol. Cell. Proteomics 8 2009 357 364
    • (2009) Mol. Cell. Proteomics , vol.8 , pp. 357-364
    • Schulz, B.L.1    Aebi, M.2
  • 35
    • 80053469048 scopus 로고    scopus 로고
    • Mechanisms and principles of N-linked protein glycosylation
    • F. Schwarz, and M. Aebi Mechanisms and principles of N-linked protein glycosylation Curr. Opin. Struct. Biol. 21 2011 576 582
    • (2011) Curr. Opin. Struct. Biol. , vol.21 , pp. 576-582
    • Schwarz, F.1    Aebi, M.2
  • 36
    • 27944459619 scopus 로고    scopus 로고
    • Yeast oligosaccharyltransferase consists of two functionally distinct sub-complexes, specified by either the Ost3p or Ost6p subunit
    • M. Schwarz, R. Knauer, and L. Lehle Yeast oligosaccharyltransferase consists of two functionally distinct sub-complexes, specified by either the Ost3p or Ost6p subunit FEBS Lett. 579 2005 6564 6568
    • (2005) FEBS Lett. , vol.579 , pp. 6564-6568
    • Schwarz, M.1    Knauer, R.2    Lehle, L.3
  • 37
    • 84876319236 scopus 로고    scopus 로고
    • Extreme C-terminal sites are posttranslocationally glycosylated by the STT3B isoform of the OST
    • S. Shrimal, S.F. Trueman, and R. Gilmore Extreme C-terminal sites are posttranslocationally glycosylated by the STT3B isoform of the OST J. Cell Biol. 201 2013 81 95
    • (2013) J. Cell Biol. , vol.201 , pp. 81-95
    • Shrimal, S.1    Trueman, S.F.2    Gilmore, R.3
  • 38
    • 84887007032 scopus 로고    scopus 로고
    • Mutations in STT3A and STT3B cause two congenital disorders of glycosylation
    • S. Shrimal, B.G. Ng, M.E. Losfeld, R. Gilmore, and H.H. Freeze Mutations in STT3A and STT3B cause two congenital disorders of glycosylation Hum. Mol. Genet. 22 2013 4638 4645
    • (2013) Hum. Mol. Genet. , vol.22 , pp. 4638-4645
    • Shrimal, S.1    Ng, B.G.2    Losfeld, M.E.3    Gilmore, R.4    Freeze, H.H.5
  • 39
    • 0029984138 scopus 로고    scopus 로고
    • Carbohydrate-carbohydrate interactions in adhesion
    • D. Spillmann, and M.M. Burger Carbohydrate-carbohydrate interactions in adhesion J. Cell. Biochem. 61 1996 562 568
    • (1996) J. Cell. Biochem. , vol.61 , pp. 562-568
    • Spillmann, D.1    Burger, M.M.2
  • 40
    • 84874640175 scopus 로고    scopus 로고
    • Loss of the oligosaccharyl transferase subunit TUSC3 promotes proliferation and migration of ovarian cancer cells
    • P. Vaňhara, P. Horak, D. Pils, M. Anees, M. Petz, W. Gregor, R. Zeillinger, and M. Krainer Loss of the oligosaccharyl transferase subunit TUSC3 promotes proliferation and migration of ovarian cancer cells Int. J. Oncol. 42 2013 1383 1389
    • (2013) Int. J. Oncol. , vol.42 , pp. 1383-1389
    • Vaňhara, P.1    Horak, P.2    Pils, D.3    Anees, M.4    Petz, M.5    Gregor, W.6    Zeillinger, R.7    Krainer, M.8
  • 41
    • 0027318961 scopus 로고
    • Biological roles of oligosaccharides: All of the theories are correct
    • A. Varki Biological roles of oligosaccharides: all of the theories are correct Glycobiology 3 1993 97 130
    • (1993) Glycobiology , vol.3 , pp. 97-130
    • Varki, A.1
  • 43
    • 33947309247 scopus 로고    scopus 로고
    • Ribophorin i acts as a substrate-specific facilitator of N-glycosylation
    • C.M. Wilson, and S. High Ribophorin I acts as a substrate-specific facilitator of N-glycosylation J. Cell Sci. 120 2007 648 657
    • (2007) J. Cell Sci. , vol.120 , pp. 648-657
    • Wilson, C.M.1    High, S.2
  • 44
    • 14244258608 scopus 로고    scopus 로고
    • Ribophorin i associates with a subset of membrane proteins after their integration at the sec61 translocon
    • C.M. Wilson, C. Kraft, C. Duggan, N. Ismail, S.G. Crawshaw, and S. High Ribophorin I associates with a subset of membrane proteins after their integration at the sec61 translocon J. Biol. Chem. 280 2005 4195 4206
    • (2005) J. Biol. Chem. , vol.280 , pp. 4195-4206
    • Wilson, C.M.1    Kraft, C.2    Duggan, C.3    Ismail, N.4    Crawshaw, S.G.5    High, S.6
  • 45
    • 47749127748 scopus 로고    scopus 로고
    • Ribophorin i regulates substrate delivery to the oligosaccharyltransferase core
    • C.M. Wilson, Q. Roebuck, and S. High Ribophorin I regulates substrate delivery to the oligosaccharyltransferase core Proc. Natl. Acad. Sci. USA 105 2008 9534 9539
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 9534-9539
    • Wilson, C.M.1    Roebuck, Q.2    High, S.3
  • 46
    • 70349449921 scopus 로고    scopus 로고
    • Mammalian MagT1 and TUSC3 are required for cellular magnesium uptake and vertebrate embryonic development
    • H. Zhou, and D.E. Clapham Mammalian MagT1 and TUSC3 are required for cellular magnesium uptake and vertebrate embryonic development Proc. Natl. Acad. Sci. USA 106 2009 15750 15755
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 15750-15755
    • Zhou, H.1    Clapham, D.E.2
  • 47
    • 77953240454 scopus 로고    scopus 로고
    • Precision mapping of an in vivo N-glycoproteome reveals rigid topological and sequence constraints
    • D.F. Zielinska, F. Gnad, J.R. Wiśniewski, and M. Mann Precision mapping of an in vivo N-glycoproteome reveals rigid topological and sequence constraints Cell 141 2010 897 907
    • (2010) Cell , vol.141 , pp. 897-907
    • Zielinska, D.F.1    Gnad, F.2    Wiśniewski, J.R.3    Mann, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.