메뉴 건너뛰기




Volumn 201, Issue 1, 2013, Pages 81-95

Extreme C-terminal sites are posttranslocationally glycosylated by the STT3B isoform of the OST

Author keywords

[No Author keywords available]

Indexed keywords

GLYCOPEPTIDE; GLYCOPROTEIN; OLIGOSACCHARYLTRANSFERASE; STT3A PROTEIN; STT3B PROTEIN; TRANSFERASE; UNCLASSIFIED DRUG;

EID: 84876319236     PISSN: 00219525     EISSN: 15408140     Source Type: Journal    
DOI: 10.1083/jcb.201301031     Document Type: Article
Times cited : (78)

References (38)
  • 1
    • 79960824997 scopus 로고    scopus 로고
    • Post-translational N-glycosylation of type I transmembrane KCNE1 peptides: implications for membrane protein biogenesis and disease
    • Bas, T., Gao G.Y., Lvov A., Chandrasekhar K.D., Gilmore R., and Kobertz W.R.. 2011. Post-translational N-glycosylation of type I transmembrane KCNE1 peptides: implications for membrane protein biogenesis and disease. Biol J.. Chem. 286:28150-28159. http://dx.doi.org/10.1074/jbc.M111.235168
    • (2011) Biol J. Chem , vol.286 , pp. 28150-28159
    • Bas, T.1    Gao, G.Y.2    Lvov, A.3    Chandrasekhar, K.D.4    Gilmore, R.5    Kobertz, W.R.6
  • 2
    • 0021256792 scopus 로고
    • Model studies on N-glycosylation of proteins
    • Bause, E. 1984. Model studies on N-glycosylation of proteins. Biochem. Soc. Trans. 12:514-517.
    • (1984) Biochem. Soc. Trans , vol.12 , pp. 514-517
    • Bause, E.1
  • 3
    • 1342306245 scopus 로고    scopus 로고
    • Biases and complex patterns in the residues flanking protein N-glycosylation sites
    • Ben-Dor, S., N. Esterman, E. Rubin, and N. Sharon. 2004. Biases and complex patterns in the residues flanking protein N-glycosylation sites. Glycobiology. 14:95-101. http://dx.doi.org/10.1093/glycob/cwh004
    • (2004) Glycobiology , vol.14 , pp. 95-101
    • Ben-Dor, S.1    Esterman, N.2    Rubin, E.3    Sharon, N.4
  • 4
    • 0026463543 scopus 로고
    • Selective removal of glycosylation sites from sex hormone-binding globulin by site-directed mutagenesis
    • Bocchinfuso, W.P., K.L. Ma, W.M. Lee, S. Warmels-Rodenhiser, and G.L. Hammond. 1992. Selective removal of glycosylation sites from sex hormone-binding globulin by site-directed mutagenesis. Endocrinology. 131:2331-2336. http://dx.doi.org/10.1210/en.131.5.2331
    • (1992) Endocrinology , vol.131 , pp. 2331-2336
    • Bocchinfuso, W.P.1    Ma, K.L.2    Lee, W.M.3    Warmels-Rodenhiser, S.4    Hammond, G.L.5
  • 5
    • 24044487195 scopus 로고    scopus 로고
    • Posttranslational N-glycosylation takes place during the normal processing of human coagulation factor VII
    • Bolt, G., C. Kristensen, and T.D. Steenstrup. 2005. Posttranslational N-glycosylation takes place during the normal processing of human coagulation factor VII. Glycobiology. 15:541-547. http://dx.doi.org/10.1093/glycob/cwi032
    • (2005) Glycobiology , vol.15 , pp. 541-547
    • Bolt, G.1    Kristensen, C.2    Steenstrup, T.D.3
  • 6
    • 69449094891 scopus 로고    scopus 로고
    • Darwinian selection for sites of Asn-linked glycosylation in phylogenetically disparate eukaryotes and viruses
    • Cui, J., T. Smith, P.W. Robbins, and J. Samuelson. 2009. Darwinian selection for sites of Asn-linked glycosylation in phylogenetically disparate eukaryotes and viruses. Proc. Natl. Acad. Sci. USA. 106:13421-13426. http://dx.doi.org/10.1073/pnas.0905818106
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 13421-13426
    • Cui, J.1    Smith, T.2    Robbins, P.W.3    Samuelson, J.4
  • 7
    • 22544467505 scopus 로고    scopus 로고
    • More than one glycan is needed for ER glucosidase II to allow entry of glycoproteins into the calnexin/calreticulin cycle
    • Deprez, P., M. Gautschi, and A. Helenius. 2005. More than one glycan is needed for ER glucosidase II to allow entry of glycoproteins into the calnexin/calreticulin cycle. Mol. Cell. 19:183-195. http://dx.doi.org/10.1016/j .molcel.2005.05.029
    • (2005) Mol. Cell , vol.19 , pp. 183-195
    • Deprez, P.1    Gautschi, M.2    Helenius, A.3
  • 8
    • 0025367812 scopus 로고
    • Sequence differences between glycosylated and non-glycosylated Asn-X-Thr/Ser acceptor sites: implications for protein engineering
    • Gavel, Y., and G. von Heijne. 1990. Sequence differences between glycosylated and non-glycosylated Asn-X-Thr/Ser acceptor sites: implications for protein engineering. Protein Eng. 3:433-442. http://dx.doi.org/10.1093/protein/3.5.433
    • (1990) Protein Eng , vol.3 , pp. 433-442
    • Gavel, Y.1    Von Heijne, G.2
  • 9
    • 71749102704 scopus 로고    scopus 로고
    • Congenital disorders of glycosylation: an update on defects affecting the biosynthesis of dolichol-linked oligosaccharides
    • Haeuptle, M.A., and T. Hennet. 2009. Congenital disorders of glycosylation: an update on defects affecting the biosynthesis of dolichol-linked oligosaccharides. Hum. Mutat. 30:1628-1641. http://dx.doi.org/10.1002/humu.21126
    • (2009) Hum. Mutat , vol.30 , pp. 1628-1641
    • Haeuptle, M.A.1    Hennet, T.2
  • 10
    • 77954266968 scopus 로고    scopus 로고
    • SATCHMO-JS: a webserver for simultaneous protein multiple sequence alignment and phylogenetic tree construction
    • Hagopian, R., J.R. Davidson, R.S. Datta, B. Samad, G.R. Jarvis, and K. Sjölander. 2010. SATCHMO-JS: a webserver for simultaneous protein multiple sequence alignment and phylogenetic tree construction. Nucleic Acids Res. 38(Suppl. 2):W29-W34. http://dx.doi.org/10.1093/nar/gkq298
    • (2010) Nucleic Acids Res , vol.38 , Issue.2 SUPPL.
    • Hagopian, R.1    Davidson, J.R.2    Datta, R.S.3    Samad, B.4    Jarvis, G.R.5    Sjölander, K.6
  • 11
    • 0025832056 scopus 로고
    • Translational control in mammalian cells
    • Hershey, J.W.B. 1991. Translational control in mammalian cells. Annu. Rev. Biochem. 60:717-755. http://dx.doi.org/10.1146/annurev.bi.60.070191.003441
    • (1991) Annu. Rev. Biochem , vol.60 , pp. 717-755
    • Hershey, J.W.B.1
  • 12
    • 76749100709 scopus 로고    scopus 로고
    • ETE: a python Environment for Tree Exploration
    • Huerta-Cepas, J., J. Dopazo, and T. Gabaldón. 2010. ETE: a python Environment for Tree Exploration. BMC Bioinformatics. 11:24. http://dx.doi.org/10.1186/1471-2105-11-24
    • (2010) BMC Bioinformatics , vol.11 , pp. 24
    • Huerta-Cepas, J.1    Dopazo, J.2    Gabaldón, T.3
  • 13
    • 38349080026 scopus 로고    scopus 로고
    • N-glycosylation site occupancy in serum glycoproteins using multiple reaction monitoring liquid chromatography-mass spectrometry
    • Hülsmeier, A.J., P. Paesold-Burda, and T. Hennet. 2007. N-glycosylation site occupancy in serum glycoproteins using multiple reaction monitoring liquid chromatography-mass spectrometry. Mol. Cell. Proteomics. 6:2132-2138. http://dx.doi.org/10.1074/mcp.M700361-MCP200
    • (2007) Mol. Cell. Proteomics , vol.6 , pp. 2132-2138
    • Hülsmeier, A.J.1    Paesold-Burda, P.2    Hennet, T.3
  • 14
    • 33645103490 scopus 로고    scopus 로고
    • An evolving view of the eukaryotic oligosaccharyltransferase
    • Kelleher, D.J., and R. Gilmore. 2006. An evolving view of the eukaryotic oligosaccharyltransferase. Glycobiology. 16:47R-62R. http://dx.doi.org/10.1093/glycob/cwj066
    • (2006) Glycobiology , vol.16
    • Kelleher, D.J.1    Gilmore, R.2
  • 15
    • 0026716017 scopus 로고
    • Oligosaccharyltransferase activity is associated with a protein complex composed of ribophorins I and II and a 48 kd protein
    • Kelleher, D.J., G. Kreibich, and R. Gilmore. 1992. Oligosaccharyltransferase activity is associated with a protein complex composed of ribophorins I and II and a 48 kd protein. Cell. 69:55-65. http://dx.doi.org/10.1016/0092-8674(92)90118-V
    • (1992) Cell , vol.69 , pp. 55-65
    • Kelleher, D.J.1    Kreibich, G.2    Gilmore, R.3
  • 16
    • 0038294237 scopus 로고    scopus 로고
    • Oligosacc haryltransferase isoforms that contain different catalytic STT3 subunits have distinct enzymatic properties
    • Kelleher, D.J., D. Karaoglu, E.C. Mandon, and R. Gilmore. 2003. Oligosacc haryltransferase isoforms that contain different catalytic STT3 subunits have distinct enzymatic properties. Mol. Cell. 12:101-111. http://dx.doi.org/10.1016/S1097-2765(03)00243-0
    • (2003) Mol. Cell , vol.12 , pp. 101-111
    • Kelleher, D.J.1    Karaoglu, D.2    Mandon, E.C.3    Gilmore, R.4
  • 17
    • 33751215862 scopus 로고    scopus 로고
    • N-linked glycosylation of folded proteins by the bacterial oligosaccharyltransferase
    • Kowarik, M., S. Numao, M.F. Feldman, B.L. Schulz, N. Callewaert, E. Kiermaier, I. Catrein, and M. Aebi. 2006. N-linked glycosylation of folded proteins by the bacterial oligosaccharyltransferase. Science. 314:1148-1150. http://dx.doi.org/10.1126/science.1134351
    • (2006) Science , vol.314 , pp. 1148-1150
    • Kowarik, M.1    Numao, S.2    Feldman, M.F.3    Schulz, B.L.4    Callewaert, N.5    Kiermaier, E.6    Catrein, I.7    Aebi, M.8
  • 18
    • 79958165964 scopus 로고    scopus 로고
    • The expanding horizons of asparagine-linked glycosylation
    • Larkin, A., and B. Imperiali. 2011. The expanding horizons of asparagine-linked glycosylation. Biochemistry. 50:4411-4426. http://dx.doi.org/10.1021/bi200346n
    • (2011) Biochemistry , vol.50 , pp. 4411-4426
    • Larkin, A.1    Imperiali, B.2
  • 19
    • 79959191882 scopus 로고    scopus 로고
    • X-ray structure of a bacterial oligosaccharyltransferase
    • Lizak, C., S. Gerber, S. Numao, M. Aebi, and K.P. Locher. 2011. X-ray structure of a bacterial oligosaccharyltransferase. Nature. 474:350-355. http://dx.doi.org/10.1038/nature10151
    • (2011) Nature , vol.474 , pp. 350-355
    • Lizak, C.1    Gerber, S.2    Numao, S.3    Aebi, M.4    Locher, K.P.5
  • 20
    • 0023941649 scopus 로고
    • The role of the asparagine-linked oligosaccharides of the alpha subunit in the secretion and assembly of human chorionic gonadotrophin
    • Matzuk, M.M., and I. Boime. 1988. The role of the asparagine-linked oligosaccharides of the alpha subunit in the secretion and assembly of human chorionic gonadotrophin. J. Cell Biol. 106:1049-1059. http://dx.doi.org/10.1083/jcb.106.4.1049
    • (1988) J. Cell Biol , vol.106 , pp. 1049-1059
    • Matzuk, M.M.1    Boime, I.2
  • 21
    • 77956036035 scopus 로고    scopus 로고
    • Specific N-linked glycosylation sites modulate synthesis and secretion of von Willebrand factor
    • McKinnon, T.A., E.C. Goode, G.M. Birdsey, A.A. Nowak, A.C. Chan, D.A. Lane, and M.A. Laffan. 2010. Specific N-linked glycosylation sites modulate synthesis and secretion of von Willebrand factor. Blood. 116:640-648. http://dx.doi.org/10.1182/blood-2010-02-267450
    • (2010) Blood , vol.116 , pp. 640-648
    • McKinnon, T.A.1    Goode, E.C.2    Birdsey, G.M.3    Nowak, A.A.4    Chan, A.C.5    Lane, D.A.6    Laffan, M.A.7
  • 22
    • 0027417476 scopus 로고
    • Determination of the distance between the oligosaccharyltransferase active site and the endoplasmic reticulum membrane
    • Nilsson, I.M., and G. von Heijne. 1993. Determination of the distance between the oligosaccharyltransferase active site and the endoplasmic reticulum membrane. J. Biol. Chem. 268:5798-5801.
    • (1993) J. Biol. Chem , vol.268 , pp. 5798-5801
    • Nilsson, I.M.1    Von Heijne, G.2
  • 23
    • 0037684809 scopus 로고    scopus 로고
    • Photocross-linking of nascent chains to the STT3 subunit of the oligosaccharyltransferase complex
    • Nilsson, I., D.J. Kelleher, Y. Miao, Y. Shao, G. Kreibich, R. Gilmore, G. von Heijne, and A.E. Johnson. 2003. Photocross-linking of nascent chains to the STT3 subunit of the oligosaccharyltransferase complex. J. Cell Biol. 161:715-725. http://dx.doi.org/10.1083/jcb.200301043
    • (2003) J. Cell Biol , vol.161 , pp. 715-725
    • Nilsson, I.1    Kelleher, D.J.2    Miao, Y.3    Shao, Y.4    Kreibich, G.5    Gilmore, R.6    von Heijne, G.7    Johnson, A.E.8
  • 24
    • 80051488226 scopus 로고    scopus 로고
    • Robust post-translocational N-glycosylation at the extreme C-terminus of membrane and secreted proteins in Xenopus laevis oocytes and HEK293 cells
    • Pult, F., G. Fallah, U. Braam, S. Detro-Dassen, C. Niculescu, B. Laube, and G. Schmalzing. 2011. Robust post-translocational N-glycosylation at the extreme C-terminus of membrane and secreted proteins in Xenopus laevis oocytes and HEK293 cells. Glycobiology. 21:1147-1160. http://dx.doi.org/10.1093/glycob/cwr013
    • (2011) Glycobiology , vol.21 , pp. 1147-1160
    • Pult, F.1    Fallah, G.2    Braam, U.3    Detro-Dassen, S.4    Niculescu, C.5    Laube, B.6    Schmalzing, G.7
  • 25
    • 58249093866 scopus 로고    scopus 로고
    • Cotranslational and posttranslational N-glycosylation of polypeptides by distinct mammalian OST isoforms
    • Ruiz-Canada, C., D.J. Kelleher, and R. Gilmore. 2009. Cotranslational and posttranslational N-glycosylation of polypeptides by distinct mammalian OST isoforms. Cell. 136:272-283. http://dx.doi.org/10.1016/j.cell.2008.11.047
    • (2009) Cell , vol.136 , pp. 272-283
    • Ruiz-Canada, C.1    Kelleher, D.J.2    Gilmore, R.3
  • 27
    • 17644366824 scopus 로고    scopus 로고
    • Proteomic analysis of mammalian oligosaccharyltransferase reveals multiple subcomplexes that contain Sec61, TRAP, and two potential new subunits
    • Shibatani, T., L.L. David, A.L. McCormack, K. Frueh, and W.R. Skach. 2005. Proteomic analysis of mammalian oligosaccharyltransferase reveals multiple subcomplexes that contain Sec61, TRAP, and two potential new subunits. Biochemistry. 44:5982-5992. http://dx.doi.org/10.1021/bi047328f
    • (2005) Biochemistry , vol.44 , pp. 5982-5992
    • Shibatani, T.1    David, L.L.2    McCormack, A.L.3    Frueh, K.4    Skach, W.R.5
  • 28
    • 0027288659 scopus 로고
    • The role of glycosylation and phosphorylation in the expression of active human beta-glucuronidase
    • Shipley, J.M., J.H. Grubb, and W.S. Sly. 1993. The role of glycosylation and phosphorylation in the expression of active human beta-glucuronidase. J. Biol. Chem. 268:12193-12198.
    • (1993) J. Biol. Chem , vol.268 , pp. 12193-12198
    • Shipley, J.M.1    Grubb, J.H.2    Sly, W.S.3
  • 29
    • 79960146847 scopus 로고    scopus 로고
    • Characterization of early EDEM1 protein maturation events and their functional implications
    • Tamura, T., J.H. Cormier, and D.N. Hebert. 2011. Characterization of early EDEM1 protein maturation events and their functional implications. J. Biol. Chem. 286:24906-24915. http://dx.doi.org/10.1074/jbc.M111.243998
    • (2011) J. Biol. Chem , vol.286 , pp. 24906-24915
    • Tamura, T.1    Cormier, J.H.2    Hebert, D.N.3
  • 31
    • 77952378813 scopus 로고    scopus 로고
    • Glutamine-linked and non-consensus asparagine-linked oligosaccharides present in human recombinant antibodies define novel protein glycosylation motifs
    • Valliere-Douglass, J.F., C.M. Eakin, A. Wallace, R.R. Ketchem, W. Wang, M.J. Treuheit, and A. Balland. 2010. Glutamine-linked and non-consensus asparagine-linked oligosaccharides present in human recombinant antibodies define novel protein glycosylation motifs. J. Biol. Chem. 285:16012-16022. http://dx.doi.org/10.1074/jbc.M109.096412
    • (2010) J. Biol. Chem , vol.285 , pp. 16012-16022
    • Valliere-Douglass, J.F.1    Eakin, C.M.2    Wallace, A.3    Ketchem, R.R.4    Wang, W.5    Treuheit, M.J.6    Balland, A.7
  • 32
    • 0030866216 scopus 로고    scopus 로고
    • Multiple dimeric forms of human CD69 result from differential addition of N-glycans to typical (Asn-X-Ser/Thr) and atypical (Asn-X-cys) glycosylation motifs
    • Vance, B.A., W. Wu, R.K. Ribaudo, D.M. Segal, and K.P. Kearse. 1997. Multiple dimeric forms of human CD69 result from differential addition of N-glycans to typical (Asn-X-Ser/Thr) and atypical (Asn-X-cys) glycosylation motifs. J. Biol. Chem. 272:23117-23122. http://dx.doi.org/10.1074/jbc.272.37.23117
    • (1997) J. Biol. Chem , vol.272 , pp. 23117-23122
    • Vance, B.A.1    Wu, W.2    Ribaudo, R.K.3    Segal, D.M.4    Kearse, K.P.5
  • 34
    • 79955488489 scopus 로고    scopus 로고
    • A 3D analysis of yeast ER structure reveals how ER domains are organized by membrane curvature
    • West, M., N. Zurek, A. Hoenger, and G.K. Voeltz. 2011. A 3D analysis of yeast ER structure reveals how ER domains are organized by membrane curvature. J. Cell Biol. 193:333-346. http://dx.doi.org/10.1083/jcb.201011039
    • (2011) J. Cell Biol , vol.193 , pp. 333-346
    • West, M.1    Zurek, N.2    Hoenger, A.3    Voeltz, G.K.4
  • 35
    • 0029983258 scopus 로고    scopus 로고
    • A nascent secretory protein may traverse the ribosome/endoplasmic reticulum translocase complex as an extended chain
    • Whitley, P., I.M. Nilsson, and G. von Heijne. 1996. A nascent secretory protein may traverse the ribosome/endoplasmic reticulum translocase complex as an extended chain. J. Biol. Chem. 271:6241-6244. http://dx.doi.org/10.1074/jbc.271.11.6241
    • (1996) J. Biol. Chem , vol.271 , pp. 6241-6244
    • Whitley, P.1    Nilsson, I.M.2    Von Heijne, G.3
  • 36
    • 0037033113 scopus 로고    scopus 로고
    • Studies on the function of oligosaccharyl transferase subunits
    • Yan, Q., and W.J. Lennarz. 2002. Studies on the function of oligosaccharyl transferase subunits. Stt3p is directly involved in the glycosylation process. J. Biol. Chem. 277:47692-47700. http://dx.doi.org/10.1074/jbc.M208136200
    • (2002) J. Biol. Chem , vol.277 , pp. 47692-47700
    • Yan, Q.1    Lennarz, W.J.2
  • 37
    • 77953240454 scopus 로고    scopus 로고
    • Precision mapping of an in vivo N-glycoproteome reveals rigid topological and sequence constraints
    • Zielinska, D.F., F. Gnad, J.R. Wiśniewski, and M. Mann. 2010. Precision mapping of an in vivo N-glycoproteome reveals rigid topological and sequence constraints. Cell. 141:897-907. http://dx.doi.org/10.1016/j.cell.2010.04.012
    • (2010) Cell , vol.141 , pp. 897-907
    • Zielinska, D.F.1    Gnad, F.2    Wiśniewski, J.R.3    Mann, M.4
  • 38
    • 84861427459 scopus 로고    scopus 로고
    • Mapping N-glycosylation sites across seven evolutionarily distant species reveals a divergent substrate proteome despite a common core machinery
    • Zielinska, D.F., F. Gnad, K. Schropp, J.R. Wiśniewski, and M. Mann. 2012. Mapping N-glycosylation sites across seven evolutionarily distant species reveals a divergent substrate proteome despite a common core machinery. Mol. Cell. 46:542-548. http://dx.doi.org/10.1016/j.molcel.2012.04.031
    • (2012) Mol. Cell , vol.46 , pp. 542-548
    • Zielinska, D.F.1    Gnad, F.2    Schropp, K.3    Wiśniewski, J.R.4    Mann, M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.