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Volumn 22, Issue 10, 2015, Pages 1301-1312

XBP1s links the unfolded protein response to the molecular architecture of mature N-glycans

Author keywords

[No Author keywords available]

Indexed keywords

GLYCAN DERIVATIVE; GLYCOPEPTIDASE; GLYCOPROTEIN; N GLYCAN DERIVATIVE; UNCLASSIFIED DRUG; X BOX BINDING PROTEIN 1; DNA BINDING PROTEIN; POLYSACCHARIDE; REGULATORY FACTOR X TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR; XBP1 PROTEIN, HUMAN;

EID: 84950241116     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.chembiol.2015.09.006     Document Type: Article
Times cited : (36)

References (53)
  • 1
    • 84880586512 scopus 로고    scopus 로고
    • N-Linked protein glycosylation in the ER
    • Aebi, M. (2013). N-Linked protein glycosylation in the ER. Biochim. Biophys. Acta 1833, 2430-2437.
    • (2013) Biochim. Biophys. Acta , vol.1833 , pp. 2430-2437
    • Aebi, M.1
  • 2
    • 77955486614 scopus 로고    scopus 로고
    • XBP1s levels are implicated in the biology and outcome of myeloma mediating different clinical outcomes to thalidomide-based treatments
    • Bagratuni, T., Wu, P., de Castro, D.G., Davenport, E.L., Dickens, N.J., Walker, B.A., Boyd, K., Johnson, D.C., Gregory, W., Morgan, G.J., et al. (2010). XBP1s levels are implicated in the biology and outcome of myeloma mediating different clinical outcomes to thalidomide-based treatments. Blood 116, 250-253.
    • (2010) Blood , vol.116 , pp. 250-253
    • Bagratuni, T.1    Wu, P.2    De Castro, D.G.3    Davenport, E.L.4    Dickens, N.J.5    Walker, B.A.6    Boyd, K.7    Johnson, D.C.8    Gregory, W.9    Morgan, G.J.10
  • 4
    • 79959481888 scopus 로고    scopus 로고
    • Protein folding and modification in the mammalian endoplasmic reticulum
    • Braakman, I., and Bulleid, N.J. (2011). Protein folding and modification in the mammalian endoplasmic reticulum. Annu. Rev. Biochem. 80, 71-99.
    • (2011) Annu. Rev. Biochem , vol.80 , pp. 71-99
    • Braakman, I.1    Bulleid, N.J.2
  • 7
    • 44849102178 scopus 로고    scopus 로고
    • Getting in and out from calnexin/calreticulin cycles
    • Caramelo, J.J., and Parodi, A.J. (2008). Getting in and out from calnexin/calreticulin cycles. J. Biol. Chem. 283, 10221-10225.
    • (2008) J. Biol. Chem , vol.283 , pp. 10221-10225
    • Caramelo, J.J.1    Parodi, A.J.2
  • 9
    • 45549094069 scopus 로고    scopus 로고
    • GlycoWorkbench: A tool for the computer-assisted annotation of mass spectra of glycans
    • Ceroni, A., Maass, K., Geyer, H., Geyer, R., Dell, A., and Haslam, S.M. (2008). GlycoWorkbench: A tool for the computer-assisted annotation of mass spectra of glycans. J. Proteome Res. 7, 1650-1659.
    • (2008) J. Proteome Res , vol.7 , pp. 1650-1659
    • Ceroni, A.1    Maass, K.2    Geyer, H.3    Geyer, R.4    Dell, A.5    Haslam, S.M.6
  • 12
    • 79551626904 scopus 로고    scopus 로고
    • Protein native-state stabilization by placing aromatic side chains in N-glycosylated reverse turns
    • Culyba, E.K., Price, J.L., Hanson, S.R., Dhar, A., Wong, C.-H., Gruebele, M., Powers, E.T., and Kelly, J.W. (2011). Protein native-state stabilization by placing aromatic side chains in N-glycosylated reverse turns. Science 331, 571-575.
    • (2011) Science , vol.331 , pp. 571-575
    • Culyba, E.K.1    Price, J.L.2    Hanson, S.R.3    Dhar, A.4    Wong, C.-H.5    Gruebele, M.6    Powers, E.T.7    Kelly, J.W.8
  • 14
    • 72249094196 scopus 로고    scopus 로고
    • Metabolism, cell surface organization, and disease
    • Dennis, J.W., Nabi, I.R., and Demetriou, M. (2009). Metabolism, cell surface organization, and disease. Cell 139, 1229-1241.
    • (2009) Cell , vol.139 , pp. 1229-1241
    • Dennis, J.W.1    Nabi, I.R.2    Demetriou, M.3
  • 16
    • 0037136405 scopus 로고    scopus 로고
    • The mannose receptor family
    • East, L., and Isacke, C.M. (2002). The mannose receptor family. Biochim. Biophys. Acta 1572, 364-386.
    • (2002) Biochim. Biophys. Acta , vol.1572 , pp. 364-386
    • East, L.1    Isacke, C.M.2
  • 17
    • 0025076063 scopus 로고
    • Kifunensine, a potent inhibitor of the glycoprotein processing mannosidase i
    • Elbein, A.D., Tropea, J.E., Mitchell, M., and Kaushal, G.P. (1990). Kifunensine, a potent inhibitor of the glycoprotein processing mannosidase I. J. Biol. Chem. 265, 15599-15605.
    • (1990) J. Biol. Chem , vol.265 , pp. 15599-15605
    • Elbein, A.D.1    Tropea, J.E.2    Mitchell, M.3    Kaushal, G.P.4
  • 20
    • 1542651212 scopus 로고    scopus 로고
    • Upregulation and overexpression of human X-box binding protein 1 (hXBP-1) gene in primary breast cancers
    • Fujimoto, T., Onda, M., Nagai, H., Nagahata, T., Ogawa, K., and Emi, M. (2003). Upregulation and overexpression of human X-box binding protein 1 (hXBP-1) gene in primary breast cancers. Breast Cancer 10, 301-306.
    • (2003) Breast Cancer , vol.10 , pp. 301-306
    • Fujimoto, T.1    Onda, M.2    Nagai, H.3    Nagahata, T.4    Ogawa, K.5    Emi, M.6
  • 21
    • 0028103695 scopus 로고
    • Role of N-linked oligosaccharide recognition, glucose trimming, and calnexin in glycoprotein folding and quality control
    • Hammond, C., Braakman, I., and Helenius, A. (1994). Role of N-linked oligosaccharide recognition, glucose trimming, and calnexin in glycoprotein folding and quality control. Proc. Natl. Acad. Sci. USA 91, 913-917.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 913-917
    • Hammond, C.1    Braakman, I.2    Helenius, A.3
  • 22
    • 80055094003 scopus 로고    scopus 로고
    • Functional organization of Golgi N- and O-glycosylation pathways involves pH-dependent complex formation that is impaired in cancer cells
    • Hassinen, A., Pujol, F.M., Kokkonen, N., Pieters, C., Kihlström, M., Korhonen, K., and Kellokumpu, S. (2011). Functional organization of Golgi N- and O-glycosylation pathways involves pH-dependent complex formation that is impaired in cancer cells. J. Biol. Chem. 286, 38329-38340.
    • (2011) J. Biol. Chem , vol.286 , pp. 38329-38340
    • Hassinen, A.1    Pujol, F.M.2    Kokkonen, N.3    Pieters, C.4    Kihlström, M.5    Korhonen, K.6    Kellokumpu, S.7
  • 23
    • 84898022102 scopus 로고    scopus 로고
    • Altered tumor-cell glycosylation promotes metastasis
    • Häuselmann, I., and Borsig, L. (2014). Altered tumor-cell glycosylation promotes metastasis. Front Oncol. 4, 28.
    • (2014) Front Oncol , vol.4 , pp. 28
    • Häuselmann, I.1    Borsig, L.2
  • 24
    • 0032714568 scopus 로고    scopus 로고
    • Importance of glycosidases in mammalian glycoprotein biosynthesis
    • Herscovics, A. (1999). Importance of glycosidases in mammalian glycoprotein biosynthesis. Biochim. Biophys. Acta 1473, 96-107.
    • (1999) Biochim. Biophys. Acta , vol.1473 , pp. 96-107
    • Herscovics, A.1
  • 25
    • 0032526093 scopus 로고    scopus 로고
    • Human α-galactosidase A: Glycosylation site 3 is essential for enzyme solubility
    • Ioannou, Y.A., Zeidner, K.M., Grace, M.E., and Desnick, R.J. (1998). Human α-galactosidase A: glycosylation site 3 is essential for enzyme solubility. Biochem. J. 332, 789-797.
    • (1998) Biochem. J , vol.332 , pp. 789-797
    • Ioannou, Y.A.1    Zeidner, K.M.2    Grace, M.E.3    Desnick, R.J.4
  • 26
    • 77956972260 scopus 로고    scopus 로고
    • A general chemical method to regulate protein stability in the mammalian central nervous system
    • Iwamoto, M., Björklund, T., Lundberg, C., Kirik, D., and Wandless, T.J. (2010). A general chemical method to regulate protein stability in the mammalian central nervous system. Chem. Biol. 17, 981-988.
    • (2010) Chem. Biol , vol.17 , pp. 981-988
    • Iwamoto, M.1    Björklund, T.2    Lundberg, C.3    Kirik, D.4    Wandless, T.J.5
  • 27
    • 0028262949 scopus 로고
    • Glycosidases in structural analysis
    • Jacob, G.S., and Scudder, P. (1994). Glycosidases in structural analysis. Methods Enzymol. 230, 280-299.
    • (1994) Methods Enzymol , vol.230 , pp. 280-299
    • Jacob, G.S.1    Scudder, P.2
  • 29
    • 33947724303 scopus 로고    scopus 로고
    • Complex N-glycan number and degree of branching cooperate to regulate cell proliferation and differentiation
    • Lau, K.S., Partridge, E.A., Grigorian, A., Silvescu, C.I., Reinhold, V.N., Demetriou, M., and Dennis, J.W. (2007). Complex N-glycan number and degree of branching cooperate to regulate cell proliferation and differentiation. Cell 129, 123-134.
    • (2007) Cell , vol.129 , pp. 123-134
    • Lau, K.S.1    Partridge, E.A.2    Grigorian, A.3    Silvescu, C.I.4    Reinhold, V.N.5    Demetriou, M.6    Dennis, J.W.7
  • 30
    • 0142059951 scopus 로고    scopus 로고
    • XBP-1 regulates a subset of endoplasmic reticulum resident chaperone genes in the unfolded protein response
    • Lee, A.-H., Iwakoshi, N.N., and Glimcher, L.H. (2003). XBP-1 regulates a subset of endoplasmic reticulum resident chaperone genes in the unfolded protein response. Mol. Cell. Biol. 23, 7448-7459.
    • (2003) Mol. Cell. Biol , vol.23 , pp. 7448-7459
    • Lee, A.-H.1    Iwakoshi, N.N.2    Glimcher, L.H.3
  • 31
    • 0017181626 scopus 로고
    • The specific site of tunicamycin inhibition in the formation of dolichol-bound N-acetylglucosamine derivatives
    • Lehle, L., and Tanner, W. (1976). The specific site of tunicamycin inhibition in the formation of dolichol-bound N-acetylglucosamine derivatives. FEBS Lett. 71, 167-170.
    • (1976) FEBS Lett , vol.71 , pp. 167-170
    • Lehle, L.1    Tanner, W.2
  • 32
    • 84862728161 scopus 로고    scopus 로고
    • Vertebrate protein glycosylation: Diversity, synthesis and function
    • Moremen, K.W., Tiemeyer, M., and Nairn, A.V. (2012). Vertebrate protein glycosylation: diversity, synthesis and function. Nat. Rev. Mol. Cell Biol. 13, 448-462.
    • (2012) Nat. Rev. Mol. Cell Biol , vol.13 , pp. 448-462
    • Moremen, K.W.1    Tiemeyer, M.2    Nairn, A.V.3
  • 34
    • 34250899722 scopus 로고    scopus 로고
    • Signal integration in the endoplasmic reticulum unfolded protein response
    • Ron, D., and Walter, P. (2007). Signal integration in the endoplasmic reticulum unfolded protein response. Nat. Rev. Mol. Cell Biol. 8, 519-529.
    • (2007) Nat. Rev. Mol. Cell Biol , vol.8 , pp. 519-529
    • Ron, D.1    Walter, P.2
  • 35
    • 58249093866 scopus 로고    scopus 로고
    • Cotranslational and posttranslational N-glycosylation of polypeptides by distinct mammalian OST isoforms
    • Ruiz-Canada, C., Kelleher, D.J., and Gilmore, R. (2009). Cotranslational and posttranslational N-glycosylation of polypeptides by distinct mammalian OST isoforms. Cell 136, 272-283.
    • (2009) Cell , vol.136 , pp. 272-283
    • Ruiz-Canada, C.1    Kelleher, D.J.2    Gilmore, R.3
  • 37
    • 22244446505 scopus 로고    scopus 로고
    • The mammalian unfolded protein response
    • Schröder, M., and Kaufman, R.J. (2005). The mammalian unfolded protein response. Annu. Rev. Biochem. 74, 739-789.
    • (2005) Annu. Rev. Biochem , vol.74 , pp. 739-789
    • Schröder, M.1    Kaufman, R.J.2
  • 38
    • 34047255890 scopus 로고    scopus 로고
    • Lectins: Carbohydrate-specific reagents and biological recognition molecules
    • Sharon, N. (2007). Lectins: Carbohydrate-specific reagents and biological recognition molecules. J. Biol. Chem. 282, 2753-2764.
    • (2007) J. Biol. Chem , vol.282 , pp. 2753-2764
    • Sharon, N.1
  • 39
    • 67650726873 scopus 로고    scopus 로고
    • Collagen structure and stability
    • Shoulders, M.D., and Raines, R.T. (2009). Collagen structure and stability. Annu. Rev. Biochem. 78, 929-958.
    • (2009) Annu. Rev. Biochem , vol.78 , pp. 929-958
    • Shoulders, M.D.1    Raines, R.T.2
  • 40
    • 84878663807 scopus 로고    scopus 로고
    • Broadly applicable methodology for the rapid and dosable small molecule-mediated regulation of transcription factors in human cells
    • Shoulders, M.D., Ryno, L.M., Cooley, C.B., Kelly, J.W., and Wiseman, R.L. (2013a). Broadly applicable methodology for the rapid and dosable small molecule-mediated regulation of transcription factors in human cells. J. Am. Chem. Soc. 135, 8129-8132.
    • (2013) J. Am. Chem. Soc , vol.135 , pp. 8129-8132
    • Shoulders, M.D.1    Ryno, L.M.2    Cooley, C.B.3    Kelly, J.W.4    Wiseman, R.L.5
  • 42
    • 17644414638 scopus 로고    scopus 로고
    • Single, context-specific glycans can target misfolded glycoproteins for ER-associated degradation
    • Spear, E.D., and Ng, D.T.W. (2005). Single, context-specific glycans can target misfolded glycoproteins for ER-associated degradation. J. Cell Biol 169, 73-82.
    • (2005) J. Cell Biol , vol.169 , pp. 73-82
    • Spear, E.D.1    Ng, D.T.W.2
  • 44
    • 84879343155 scopus 로고    scopus 로고
    • XBP-1 is a cell-nonautonomous regulator of stress resistance and longevity
    • Taylor, R.C., and Dillin, A. (2013). XBP-1 is a cell-nonautonomous regulator of stress resistance and longevity. Cell 153, 1435-1447.
    • (2013) Cell , vol.153 , pp. 1435-1447
    • Taylor, R.C.1    Dillin, A.2
  • 45
    • 84855496731 scopus 로고    scopus 로고
    • The unfolded protein response supports cellular robustness as a broad-spectrum compensatory pathway
    • Thibault, G., Ismail, N., and Ng, D.T.W. (2011). The unfolded protein response supports cellular robustness as a broad-spectrum compensatory pathway. Proc. Natl. Acad. Sci. USA 108, 20597-20602.
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 20597-20602
    • Thibault, G.1    Ismail, N.2    Ng, D.T.W.3
  • 46
    • 33646078130 scopus 로고    scopus 로고
    • XBP1-based engineering of secretory capacity enhances the productivity of Chinese hamster ovary cells
    • Tigges, M., and Fussenegger, M. (2006). XBP1-based engineering of secretory capacity enhances the productivity of Chinese hamster ovary cells. Metab. Eng. 8, 264-272.
    • (2006) Metab. Eng , vol.8 , pp. 264-272
    • Tigges, M.1    Fussenegger, M.2
  • 47
    • 0020469388 scopus 로고
    • Swainsonine inhibits the biosynthesis of complex glycoproteins by inhibition of Golgi mannosidase II
    • Tulsiani, D.R.P., Harris, T.M., and Touster, O. (1982). Swainsonine inhibits the biosynthesis of complex glycoproteins by inhibition of Golgi mannosidase II. J. Biol. Chem. 257, 7936-7939.
    • (1982) J. Biol. Chem , vol.257 , pp. 7936-7939
    • Tulsiani, D.R.P.1    Harris, T.M.2    Touster, O.3
  • 48
    • 84923197393 scopus 로고    scopus 로고
    • Glycosylation profiles determine extravasation and disease-targeting properties of armed antibodies
    • Venetz, D., Hess, C., Lin, C.-W., Aebi, M., and Neri, D. (2015). Glycosylation profiles determine extravasation and disease-targeting properties of armed antibodies. Proc. Natl. Acad. Sci. USA 112, 2000-2005.
    • (2015) Proc. Natl. Acad. Sci. USA , vol.112 , pp. 2000-2005
    • Venetz, D.1    Hess, C.2    Lin, C.-W.3    Aebi, M.4    Neri, D.5
  • 50
    • 82255173966 scopus 로고    scopus 로고
    • The unfolded protein response: From stress pathway to homeostatic regulation
    • Walter, P., and Ron, D. (2011). The unfolded protein response: From stress pathway to homeostatic regulation. Science 334, 1081-1086.
    • (2011) Science , vol.334 , pp. 1081-1086
    • Walter, P.1    Ron, D.2
  • 51
    • 84896382541 scopus 로고    scopus 로고
    • Spliced X-box binding protein 1 couples the unfolded protein response to hexosamine biosynthetic pathway
    • Wang, Z.V., Deng, Y., Gao, N., Pedrozo, Z., Li, D.L., Morales, C.R., Criollo, A., Luo, X., Tan, W., Jiang, N., et al. (2014). Spliced X-box binding protein 1 couples the unfolded protein response to hexosamine biosynthetic pathway. Cell 156, 1179-1192.
    • (2014) Cell , vol.156 , pp. 1179-1192
    • Wang, Z.V.1    Deng, Y.2    Gao, N.3    Pedrozo, Z.4    Li, D.L.5    Morales, C.R.6    Criollo, A.7    Luo, X.8    Tan, W.9    Jiang, N.10
  • 52
    • 1842581899 scopus 로고    scopus 로고
    • N-Glycosylation is crucial for folding, trafficking, and stability of human tripeptidyl- peptidase i
    • Wujek, P., Kida, E., Walus, M., Wisniewski, K.E., and Golabek, A.A. (2004). N-Glycosylation is crucial for folding, trafficking, and stability of human tripeptidyl- peptidase I. J. Biol. Chem. 279, 12827-12839.
    • (2004) J. Biol. Chem , vol.279 , pp. 12827-12839
    • Wujek, P.1    Kida, E.2    Walus, M.3    Wisniewski, K.E.4    Golabek, A.A.5
  • 53
    • 77953240454 scopus 로고    scopus 로고
    • Precision mapping of an in vivo N-glycoproteome reveals rigid topological and sequence constraints
    • Zielinska, D.F., Gnad, F., Wis̈niewski, J.R., and Mann, M. (2010). Precision mapping of an in vivo N-glycoproteome reveals rigid topological and sequence constraints. Cell 141, 897-907.
    • (2010) Cell , vol.141 , pp. 897-907
    • Zielinska, D.F.1    Gnad, F.2    Wis̈niewski, J.R.3    Mann, M.4


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