메뉴 건너뛰기




Volumn 10, Issue 11, 2014, Pages 902-910

The intrinsic and extrinsic effects of N-linked glycans on glycoproteostasis

Author keywords

[No Author keywords available]

Indexed keywords

ASPARAGINE; GLYCAN; GLYCOPROTEIN; POLYSACCHARIDE;

EID: 84921850497     PISSN: 15524450     EISSN: 15524469     Source Type: Journal    
DOI: 10.1038/nchembio.1651     Document Type: Review
Times cited : (159)

References (99)
  • 2
  • 3
    • 82255173966 scopus 로고    scopus 로고
    • The unfolded protein response: From stress pathway to homeostatic regulation
    • Walter, P. & Ron, D. The unfolded protein response: from stress pathway to homeostatic regulation. Science 334, 1081-1086 (2011).
    • (2011) Science , vol.334 , pp. 1081-1086
    • Walter, P.1    Ron, D.2
  • 4
    • 22244446505 scopus 로고    scopus 로고
    • The mammalian unfolded protein response
    • Schröder, M. & Kaufman, R. J. The mammalian unfolded protein response. Annu. Rev. Biochem. 74, 739-789 (2005).
    • (2005) Annu. Rev. Biochem. , vol.74 , pp. 739-789
    • Schröder, M.1    Kaufman, R.J.2
  • 5
    • 0032754473 scopus 로고    scopus 로고
    • On the frequency of protein glycosylation, as deduced from analysis of the SWISS-PROT database
    • Apweiler, R., Hermjakob, H. & Sharon, N. On the frequency of protein glycosylation, as deduced from analysis of the SWISS-PROT database. Biochim. Biophys. Acta 1473, 4-8 (1999).
    • (1999) Biochim. Biophys. Acta , vol.1473 , pp. 4-8
    • Apweiler, R.1    Hermjakob, H.2    Sharon, N.3
  • 6
    • 84893734160 scopus 로고    scopus 로고
    • Solving glycosylation disorders: Fundamental approaches reveal complicated pathways
    • Freeze, H. H., Chong, J. X., Bamshad, M. J. & Ng, B. G. Solving glycosylation disorders: fundamental approaches reveal complicated pathways. Am. J. Hum. Genet. 94, 161-175 (2014).
    • (2014) Am. J. Hum. Genet. , vol.94 , pp. 161-175
    • Freeze, H.H.1    Chong, J.X.2    Bamshad, M.J.3    Ng, B.G.4
  • 7
    • 58249093866 scopus 로고    scopus 로고
    • Cotranslational and posttranslational N-glycosylation of polypeptides by distinct mammalian OST isoforms
    • Ruiz-Canada, C., Kelleher, D. J. & Gilmore, R. Cotranslational and posttranslational N-glycosylation of polypeptides by distinct mammalian OST isoforms. Cell 136, 272-283 (2009). Identification of a new active site subunit for the OST that is capable of modifying proteins post-translationally.
    • (2009) Cell , vol.136 , pp. 272-283
    • Ruiz-Canada, C.1    Kelleher, D.J.2    Gilmore, R.3
  • 8
    • 0032146060 scopus 로고    scopus 로고
    • A molecular basis for glycosylation-induced conformational switching
    • O'Conner, S. E. & Imperiali, B. A molecular basis for glycosylation-induced conformational switching. Chem. Biol. 5, 427-437 (1998).
    • (1998) Chem. Biol. , vol.5 , pp. 427-437
    • O'Conner, S.E.1    Imperiali, B.2
  • 9
    • 84864841234 scopus 로고    scopus 로고
    • N-glycosylation of enhanced aromatic sequons to increase glycoprotein stability
    • Price, J. L. et al. N-glycosylation of enhanced aromatic sequons to increase glycoprotein stability. Biopolymers 98, 195-211 (2012).
    • (2012) Biopolymers , vol.98 , pp. 195-211
    • Price, J.L.1
  • 10
    • 67449119292 scopus 로고    scopus 로고
    • Effects of glycosylation on the stability of protein pharmaceuticals
    • Solá, R. J. & Griebenow, K. Effects of glycosylation on the stability of protein pharmaceuticals. J. Pharm. Sci. 98, 1223-1245 (2009).
    • (2009) J. Pharm. Sci. , vol.98 , pp. 1223-1245
    • Solá, R.J.1    Griebenow, K.2
  • 11
    • 84866623060 scopus 로고    scopus 로고
    • Flagging and docking: Dual roles for N-glycans in protein quality control and cellular proteostasis
    • Hebert, D. N. & Molinari, M. Flagging and docking: dual roles for N-glycans in protein quality control and cellular proteostasis. Trends Biochem. Sci. 37, 404-410 (2012).
    • (2012) Trends Biochem. Sci. , vol.37 , pp. 404-410
    • Hebert, D.N.1    Molinari, M.2
  • 12
    • 0031758846 scopus 로고    scopus 로고
    • A structural role for glycosylation: Lessons from the hp model
    • Hoffmann, D. & Florke, H. A structural role for glycosylation: lessons from the hp model. Fold. Des. 3, 337-343 (1998).
    • (1998) Fold. Des. , vol.3 , pp. 337-343
    • Hoffmann, D.1    Florke, H.2
  • 13
    • 46149089907 scopus 로고    scopus 로고
    • Effect of glycosylation on protein folding: A close look at thermodynamic stabilization
    • Shental-Bechor, D. & Levy, Y. Effect of glycosylation on protein folding: a close look at thermodynamic stabilization. Proc. Natl. Acad. Sci. USA 105, 8256-8261 (2008).
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 8256-8261
    • Shental-Bechor, D.1    Levy, Y.2
  • 14
    • 0025782587 scopus 로고
    • The conformational effects of N-glycosylation on the tailpiece from serum IgM
    • Wormald, M. R. et al. The conformational effects of N-glycosylation on the tailpiece from serum IgM. Eur. J. Biochem. 198, 131-139 (1991).
    • (1991) Eur. J. Biochem. , vol.198 , pp. 131-139
    • Wormald, M.R.1
  • 15
    • 0036586477 scopus 로고    scopus 로고
    • Chaperone-like functions of N-glycans in the formation and stabilization of protein conformation
    • Yamaguchi, H. Chaperone-like functions of N-glycans in the formation and stabilization of protein conformation. Trends Glycosci. Glycotechnol. 14, 139-151 (2002).
    • (2002) Trends Glycosci. Glycotechnol. , vol.14 , pp. 139-151
    • Yamaguchi, H.1
  • 16
    • 78651099872 scopus 로고    scopus 로고
    • Perturbing the folding energy landscape of the bacterial immunity protein Im7 by site-specific N-linked glycosylation
    • Chen, M. M. et al. Perturbing the folding energy landscape of the bacterial immunity protein Im7 by site-specific N-linked glycosylation. Proc. Natl. Acad. Sci. USA 107, 22528-22533 (2010).
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 22528-22533
    • Chen, M.M.1
  • 17
    • 78049400651 scopus 로고    scopus 로고
    • Context-dependent effects of asparagine glycosylation on Pin WW folding kinetics and thermodynamics
    • Price, J. L. et al. Context-dependent effects of asparagine glycosylation on Pin WW folding kinetics and thermodynamics. J. Am. Chem. Soc. 132, 15359-15367 (2010).
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 15359-15367
    • Price, J.L.1
  • 18
    • 77956275854 scopus 로고    scopus 로고
    • Intramolecular glycan-protein interactions in glycoproteins
    • Barb, A. W., Borgert, A. J., Liu, M., Barany, G. & Live, D. Intramolecular glycan-protein interactions in glycoproteins. Methods Enzymol. 478, 365-388 (2010).
    • (2010) Methods Enzymol. , vol.478 , pp. 365-388
    • Barb, A.W.1    Borgert, A.J.2    Liu, M.3    Barany, G.4    Live, D.5
  • 19
    • 84911304823 scopus 로고
    • Protein-carbohydrate interactions-basic molecular features
    • Quiocho, F. A. Protein-carbohydrate interactions-basic molecular features. Pure Appl. Chem. 61, 1293-1306 (1989).
    • (1989) Pure Appl. Chem. , vol.61 , pp. 1293-1306
    • Quiocho, F.A.1
  • 20
    • 0003012148 scopus 로고    scopus 로고
    • How water provides the impetus for molecular recognition in aqueous solution
    • Lemieux, R. U. How water provides the impetus for molecular recognition in aqueous solution. Acc. Chem. Res. 29, 373-380 (1996).
    • (1996) Acc. Chem. Res. , vol.29 , pp. 373-380
    • Lemieux, R.U.1
  • 22
    • 67650340734 scopus 로고    scopus 로고
    • Localized thermodynamic coupling between hydrogen bonding and microenvironment polarity substantially stabilizes proteins
    • Gao, J., Bosco, D. A., Powers, E. T. & Kelly, J. W. Localized thermodynamic coupling between hydrogen bonding and microenvironment polarity substantially stabilizes proteins. Nat. Struct. Mol. Biol. 16, 684-690 (2009).
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 684-690
    • Gao, J.1    Bosco, D.A.2    Powers, E.T.3    Kelly, J.W.4
  • 23
    • 0037474543 scopus 로고    scopus 로고
    • Structural analysis of human IgG-Fc glycoforms reveals a correlation between glycosylation and structural integrity
    • Krapp, S., Mimura, Y., Jefferis, R., Huber, R. & Sondermann, P. Structural analysis of human IgG-Fc glycoforms reveals a correlation between glycosylation and structural integrity. J. Mol. Biol. 325, 979-989 (2003).
    • (2003) J. Mol. Biol. , vol.325 , pp. 979-989
    • Krapp, S.1    Mimura, Y.2    Jefferis, R.3    Huber, R.4    Sondermann, P.5
  • 24
    • 84879772775 scopus 로고    scopus 로고
    • Structural and energetic basis of carbohydrate-aromatic packing interactions in proteins
    • Chen, W. et al. Structural and energetic basis of carbohydrate-aromatic packing interactions in proteins. J. Am. Chem. Soc. 135, 9877-9884 (2013).
    • (2013) J. Am. Chem. Soc. , vol.135 , pp. 9877-9884
    • Chen, W.1
  • 25
    • 66549116707 scopus 로고    scopus 로고
    • Heat capacity changes in carbohydrates and protein-carbohydrate complexes
    • Chavelas, E. A. & Garcia-Hernandez, E. Heat capacity changes in carbohydrates and protein-carbohydrate complexes. Biochem. J. 420, 239-247 (2009).
    • (2009) Biochem. J. , vol.420 , pp. 239-247
    • Chavelas, E.A.1    Garcia-Hernandez, E.2
  • 26
    • 0028773646 scopus 로고
    • Structure of human chorionic gonadotropin at 2.6 Å resolution from MAD analysis of the selenomethionyl protein
    • Wu, H., Lustbader, J. W., Liu, Y., Canfield, R. E. & Hendrickson, W. A. Structure of human chorionic gonadotropin at 2.6 Å resolution from MAD analysis of the selenomethionyl protein. Structure 2, 545-558 (1994).
    • (1994) Structure , vol.2 , pp. 545-558
    • Wu, H.1    Lustbader, J.W.2    Liu, Y.3    Canfield, R.E.4    Hendrickson, W.A.5
  • 27
    • 0029952519 scopus 로고    scopus 로고
    • Structural basis of lectin-carbohydrate recognition
    • Weis, W. I. & Drickamer, K. Structural basis of lectin-carbohydrate recognition. Annu. Rev. Biochem. 65, 441-473 (1996).
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 441-473
    • Weis, W.I.1    Drickamer, K.2
  • 28
    • 1342327544 scopus 로고    scopus 로고
    • Statistical analysis of the protein environment of N-glycosylation sites: Implications for occupancy, structure, and folding
    • Petrescu, A. J., Milac, A. L., Petrescu, S. M., Dwek, R. A. & Wormald, M. R. Statistical analysis of the protein environment of N-glycosylation sites: implications for occupancy, structure, and folding. Glycobiology 14, 103-114 (2004). Very informative survey of the protein primary, secondary and tertiary structural environments that surround N-linked glycans based on a database of glycoprotein crystal structures.
    • (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
  • 29
    • 84939652478 scopus 로고    scopus 로고
    • ed. Petrescu, S. M., InTech, Additional helpful survey of structural environment of N-linked glycans
    • Surleac, M. D. et al. in Glycosylation (ed. Petrescu, S. M.) 3-20 (InTech, 2012). Additional helpful survey of structural environment of N-linked glycans.
    • (2012) Glycosylation , pp. 3-20
    • Surleac, M.D.1
  • 30
    • 79960935413 scopus 로고    scopus 로고
    • The CH/π hydrogen bond in chemistry. Conformation, supramolecules, optical resolution and interactions involving carbohydrates
    • Nishio, M. The CH/π hydrogen bond in chemistry. Conformation, supramolecules, optical resolution and interactions involving carbohydrates. Phys. Chem. Chem. Phys. 13, 13873-13900 (2011).
    • (2011) Phys. Chem. Chem. Phys. , vol.13 , pp. 13873-13900
    • Nishio, M.1
  • 31
    • 62549107841 scopus 로고    scopus 로고
    • The core trisaccharide of an N-linked glycoprotein intrinsically accelerates folding and enhances stability
    • Hanson, S. R. et al. The core trisaccharide of an N-linked glycoprotein intrinsically accelerates folding and enhances stability. Proc. Natl. Acad. Sci. USA 106, 3131-3136 (2009).
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 3131-3136
    • Hanson, S.R.1
  • 32
    • 79551626904 scopus 로고    scopus 로고
    • Protein native-state stabilization by placing aromatic side chains in N-glycosylated reverse turns
    • Culyba, E. K. et al. Protein native-state stabilization by placing aromatic side chains in N-glycosylated reverse turns. Science 331, 571-575 (2011). This article introduced the enhanced aromatic sequon, an N-glycosylated structural module that stabilizes the proteins in which it is found and appears to be glycosylated with unusually high efficiency by OST.
    • (2011) Science , vol.331 , pp. 571-575
    • Culyba, E.K.1
  • 33
    • 80052179739 scopus 로고    scopus 로고
    • Glycosylation of the enhanced aromatic sequon is similarly stabilizing in three distinct reverse turn contexts
    • Price, J. L., Powers, D. L., Powers, E. T. & Kelly, J. W. Glycosylation of the enhanced aromatic sequon is similarly stabilizing in three distinct reverse turn contexts. Proc. Natl. Acad. Sci. USA 108, 14127-14132 (2011).
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 14127-14132
    • Price, J.L.1    Powers, D.L.2    Powers, E.T.3    Kelly, J.W.4
  • 34
    • 0029133626 scopus 로고
    • Conformation and function of the N-linked glycan in the adhesion domain of human CD2
    • Wyss, D. F. et al. Conformation and function of the N-linked glycan in the adhesion domain of human CD2. Science 269, 1273-1278 (1995).
    • (1995) Science , vol.269 , pp. 1273-1278
    • Wyss, D.F.1
  • 35
    • 64049096002 scopus 로고    scopus 로고
    • N-glycans are direct determinants of CFTR folding and stability in secretory and endocytic membrane traffic
    • Glozman, R. et al. N-glycans are direct determinants of CFTR folding and stability in secretory and endocytic membrane traffic. J. Cell Biol. 184, 847-862 (2009).
    • (2009) J. Cell Biol. , vol.184 , pp. 847-862
    • Glozman, R.1
  • 36
    • 72849107561 scopus 로고    scopus 로고
    • The role of rhodopsin glycosylation in protein folding, trafficking, and light-sensitive retinal degeneration
    • Tam, B. M. & Moritz, O. L. The role of rhodopsin glycosylation in protein folding, trafficking, and light-sensitive retinal degeneration. J. Neurosci. 29, 15145-15154 (2009).
    • (2009) J. Neurosci. , vol.29 , pp. 15145-15154
    • Tam, B.M.1    Moritz, O.L.2
  • 37
    • 40849088166 scopus 로고    scopus 로고
    • Identification of ERGIC-53 as an intracellular transport receptor of α1-antitrypsin
    • Nyfeler, B. et al. Identification of ERGIC-53 as an intracellular transport receptor of α1-antitrypsin. J. Cell Biol. 180, 705-712 (2008).
    • (2008) J. Cell Biol. , vol.180 , pp. 705-712
    • Nyfeler, B.1
  • 38
    • 44849102178 scopus 로고    scopus 로고
    • Getting in and out from calnexin/calreticulin cycles
    • Caramelo, J. J. & Parodi, A. J. Getting in and out from calnexin/calreticulin cycles. J. Biol. Chem. 283, 10221-10225 (2008).
    • (2008) J. Biol. Chem. , vol.283 , pp. 10221-10225
    • Caramelo, J.J.1    Parodi, A.J.2
  • 39
    • 0037458633 scopus 로고    scopus 로고
    • Interactions of substrate with calreticulin, an endoplasmic reticulum chaperone
    • Kapoor, M. et al. Interactions of substrate with calreticulin, an endoplasmic reticulum chaperone. J. Biol. Chem. 278, 6194-6200 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 6194-6200
    • Kapoor, M.1
  • 40
    • 0034799402 scopus 로고    scopus 로고
    • The structure of calnexin, an ER chaperone involved in quality control of protein folding
    • Schrag, J. D. et al. The structure of calnexin, an ER chaperone involved in quality control of protein folding. Mol. Cell 8, 633-644 (2001).
    • (2001) Mol. Cell , vol.8 , pp. 633-644
    • Schrag, J.D.1
  • 41
    • 0037133347 scopus 로고    scopus 로고
    • TROSY-NMR reveals interaction between ERp57 and the tip of the calreticulin P-domain
    • Frickel, E. M. et al. TROSY-NMR reveals interaction between ERp57 and the tip of the calreticulin P-domain. Proc. Natl. Acad. Sci. USA 99, 1954-1959 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 1954-1959
    • Frickel, E.M.1
  • 42
    • 78649641361 scopus 로고    scopus 로고
    • Structural basis of carbohydrate recognition by calreticulin
    • Kozlov, G. et al. Structural basis of carbohydrate recognition by calreticulin. J. Biol. Chem. 285, 38612-38620 (2010).
    • (2010) J. Biol. Chem. , vol.285 , pp. 38612-38620
    • Kozlov, G.1
  • 43
    • 0029934119 scopus 로고    scopus 로고
    • Calnexin and calreticulin promote folding, delay oligomerization and suppress degradation of influenza hemagglutinin in microsomes
    • Hebert, D. N., Foellmer, B. & Helenius, A. Calnexin and calreticulin promote folding, delay oligomerization and suppress degradation of influenza hemagglutinin in microsomes. EMBO J. 15, 2961-2968 (1996).
    • (1996) EMBO J. , vol.15 , pp. 2961-2968
    • Hebert, D.N.1    Foellmer, B.2    Helenius, A.3
  • 44
    • 0029925940 scopus 로고    scopus 로고
    • The molecular chaperone calnexin facilitates folding and assembly of class I histocompatibility molecules
    • Vassilakos, A., Cohen-Doyle, M. F., Peterson, P. A., Jackson, M. R. & Williams, D. B. The molecular chaperone calnexin facilitates folding and assembly of class I histocompatibility molecules. EMBO J. 15, 1495-1506 (1996).
    • (1996) EMBO J. , vol.15 , pp. 1495-1506
    • Vassilakos, A.1    Cohen-Doyle, M.F.2    Peterson, P.A.3    Jackson, M.R.4    Williams, D.B.5
  • 45
    • 0037245727 scopus 로고    scopus 로고
    • N-linked glycans direct the cotranslational folding pathway of influenza hemagglutinin
    • Daniels, R., Kurowski, B., Johnson, A. E. & Hebert, D. N. N-linked glycans direct the cotranslational folding pathway of influenza hemagglutinin. Mol. Cell 11, 79-90 (2003). Describes a detailed model for the molecular choreography for nascent glycoprotein maturation and its interaction with ER lectin chaperones.
    • (2003) Mol. Cell , vol.11 , pp. 79-90
    • Daniels, R.1    Kurowski, B.2    Johnson, A.E.3    Hebert, D.N.4
  • 46
    • 77953024704 scopus 로고    scopus 로고
    • Lectin chaperones help direct the maturation of glycoproteins in the endoplasmic reticulum
    • Pearse, B. R. & Hebert, D. N. Lectin chaperones help direct the maturation of glycoproteins in the endoplasmic reticulum. Biochim. Biophys. Acta 1803, 684-693 (2010).
    • (2010) Biochim. Biophys. Acta , vol.1803 , pp. 684-693
    • Pearse, B.R.1    Hebert, D.N.2
  • 47
    • 77953164923 scopus 로고    scopus 로고
    • The role of UDP-Glc: Glycoprotein glucosyltransferase 1 in the maturation of an obligate substrate prosaposin
    • Pearse, B. R. et al. The role of UDP-Glc: glycoprotein glucosyltransferase 1 in the maturation of an obligate substrate prosaposin. J. Cell Biol. 189, 829-841 (2010).
    • (2010) J. Cell Biol. , vol.189 , pp. 829-841
    • Pearse, B.R.1
  • 48
    • 0029024748 scopus 로고
    • Glucose trimming and reglucosylation determine glycoprotein association with calnexin in the endoplasmic reticulum
    • Hebert, D. N., Foellmer, B. & Helenius, A. Glucose trimming and reglucosylation determine glycoprotein association with calnexin in the endoplasmic reticulum. Cell 81, 425-433 (1995).
    • (1995) Cell , vol.81 , pp. 425-433
    • Hebert, D.N.1    Foellmer, B.2    Helenius, A.3
  • 49
    • 63649090633 scopus 로고    scopus 로고
    • Distinct contributions of the lectin and arm domains of calnexin to its molecular chaperone function
    • Brockmeier, A., Brockmeier, U. & Williams, D. B. Distinct contributions of the lectin and arm domains of calnexin to its molecular chaperone function. J. Biol. Chem. 284, 3433-3444 (2009).
    • (2009) J. Biol. Chem. , vol.284 , pp. 3433-3444
    • Brockmeier, A.1    Brockmeier, U.2    Williams, D.B.3
  • 50
    • 84890280767 scopus 로고    scopus 로고
    • Glycan-dependent and -independent interactions contribute to cellular substrate recruitment by calreticulin
    • Wijeyesakere, S. J., Rizvi, S. M. & Raghavan, M. Glycan-dependent and -independent interactions contribute to cellular substrate recruitment by calreticulin. J. Biol. Chem. 288, 35104-35116 (2013).
    • (2013) J. Biol. Chem. , vol.288 , pp. 35104-35116
    • Wijeyesakere, S.J.1    Rizvi, S.M.2    Raghavan, M.3
  • 51
    • 0033597829 scopus 로고    scopus 로고
    • Bulk flow redux?
    • Warren, G. & Mellman, I. Bulk flow redux? Cell 98, 125-127 (1999).
    • (1999) Cell , vol.98 , pp. 125-127
    • Warren, G.1    Mellman, I.2
  • 52
    • 38349136210 scopus 로고    scopus 로고
    • Molecular basis of sugar recognition by the human L-type lectins ERGIC-53, VIPL, and VIP36
    • Kamiya, Y. et al. Molecular basis of sugar recognition by the human L-type lectins ERGIC-53, VIPL, and VIP36. J. Biol. Chem. 283, 1857-1861 (2008).
    • (2008) J. Biol. Chem. , vol.283 , pp. 1857-1861
    • Kamiya, Y.1
  • 53
    • 0032478548 scopus 로고    scopus 로고
    • Mutations in the ER-Golgi intermediate compartment protein ERGIC-53 cause combined deficiency of coagulation factors V and VIII
    • Nichols, W. C. et al. Mutations in the ER-Golgi intermediate compartment protein ERGIC-53 cause combined deficiency of coagulation factors V and VIII. Cell 93, 61-70 (1998).
    • (1998) Cell , vol.93 , pp. 61-70
    • Nichols, W.C.1
  • 54
    • 35748948975 scopus 로고    scopus 로고
    • In and out of the ER: Protein folding, quality control, degradation, and related human diseases
    • Hebert, D. N. & Molinari, M. In and out of the ER: protein folding, quality control, degradation, and related human diseases. Physiol. Rev. 87, 1377-1408 (2007).
    • (2007) Physiol. Rev. , vol.87 , pp. 1377-1408
    • Hebert, D.N.1    Molinari, M.2
  • 55
    • 84880618745 scopus 로고    scopus 로고
    • How early studies on secreted and membrane protein quality control gave rise to the ER associated degradation (ERAD) pathway: The early history of ERAD
    • Needham, P. G. & Brodsky, J. L. How early studies on secreted and membrane protein quality control gave rise to the ER associated degradation (ERAD) pathway: the early history of ERAD. Biochim. Biophys. Acta 1833, 2447-2457 (2013).
    • (2013) Biochim. Biophys. Acta , vol.1833 , pp. 2447-2457
    • Needham, P.G.1    Brodsky, J.L.2
  • 56
    • 0034925391 scopus 로고    scopus 로고
    • N-glycan structure of a short-lived variant of ribophorin I expressed in the MadIA214 glycosylation-defective cell line reveals the role of a mannosidase that is not ER mannosidase I in the process of glycoprotein degradation
    • Ermonval, M., Kitzmuller, C., Mir, A. M., Cacan, R. & Ivessa, N. E. N-glycan structure of a short-lived variant of ribophorin I expressed in the MadIA214 glycosylation-defective cell line reveals the role of a mannosidase that is not ER mannosidase I in the process of glycoprotein degradation. Glycobiology 11, 565-576 (2001).
    • (2001) Glycobiology , vol.11 , pp. 565-576
    • Ermonval, M.1    Kitzmuller, C.2    Mir, A.M.3    Cacan, R.4    Ivessa, N.E.5
  • 57
    • 0141706616 scopus 로고    scopus 로고
    • Endoplasmic reticulum-associated degradation of mammalian glycoproteins involves sugar chain trimming to Man6-5GlcNAc2
    • Frenkel, Z., Gregory, W., Kornfeld, S. & Lederkremer, G. Z. Endoplasmic reticulum-associated degradation of mammalian glycoproteins involves sugar chain trimming to Man6-5GlcNAc2. J. Biol. Chem. 278, 34119-34124 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 34119-34124
    • Frenkel, Z.1    Gregory, W.2    Kornfeld, S.3    Lederkremer, G.Z.4
  • 58
    • 20444429745 scopus 로고    scopus 로고
    • A window of opportunity: Timing protein degradation by trimming of sugars and ubiquitins
    • Lederkremer, G. Z. & Glickman, M. H. A window of opportunity: timing protein degradation by trimming of sugars and ubiquitins. Trends Biochem. Sci. 30, 297-303 (2005).
    • (2005) Trends Biochem. Sci. , vol.30 , pp. 297-303
    • Lederkremer, G.Z.1    Glickman, M.H.2
  • 59
    • 84899436172 scopus 로고    scopus 로고
    • Golgi-localized mannosidase (MAN1B1) plays a non-enzymatic gatekeeper role in protein biosynthetic quality control
    • Iannotti, M. J., Figard, L., Sokac, A. M. & Sifers, R. N. A. Golgi-localized mannosidase (MAN1B1) plays a non-enzymatic gatekeeper role in protein biosynthetic quality control. J. Biol. Chem. 289, 11844-11858 (2014).
    • (2014) J. Biol. Chem. , vol.289 , pp. 11844-11858
    • Iannotti, M.J.1    Figard, L.2    Sokac, A.M.3    Sifers, R.N.A.4
  • 60
    • 84876557175 scopus 로고    scopus 로고
    • Golgi-situated endoplasmic reticulum α-1, 2-mannosidase contributes to the retrieval of ERAD substrates through a direct interaction with gamma-COP
    • Pan, S., Cheng, X. & Sifers, R. N. Golgi-situated endoplasmic reticulum α-1, 2-mannosidase contributes to the retrieval of ERAD substrates through a direct interaction with gamma-COP. Mol. Biol. Cell 24, 1111-1121 (2013). Provocative support for Man1B1 actually residing in the Golgi.
    • (2013) Mol. Biol. Cell , vol.24 , pp. 1111-1121
    • Pan, S.1    Cheng, X.2    Sifers, R.N.3
  • 61
    • 84892685784 scopus 로고    scopus 로고
    • MAN1B1 deficiency: An unexpected CDG-II
    • Rymen, D. et al. MAN1B1 deficiency: an unexpected CDG-II. PLoS Genet. 9, e1003989 (2013).
    • (2013) PLoS Genet. , vol.9 , pp. e1003989
    • Rymen, D.1
  • 62
    • 67650535999 scopus 로고    scopus 로고
    • Human OS-9, a lectin required for glycoprotein ERAD, recognizes mannose-trimmed N-glycans
    • Hosokawa, N., Kamiya, Y., Kamiya, D., Kato, K. & Nagata, K. Human OS-9, a lectin required for glycoprotein ERAD, recognizes mannose-trimmed N-glycans. J. Biol. Chem. 284, 17061-17068 (2009).
    • (2009) J. Biol. Chem. , vol.284 , pp. 17061-17068
    • Hosokawa, N.1    Kamiya, Y.2    Kamiya, D.3    Kato, K.4    Nagata, K.5
  • 63
    • 84875364799 scopus 로고    scopus 로고
    • Endoplasmic reticulum lectin XTP3-B inhibits endoplasmic reticulum-associated degradation of a misfolded α1-antitrypsin variant
    • Fujimori, T., Kamiya, Y., Nagata, K., Kato, K. & Hosokawa, N. Endoplasmic reticulum lectin XTP3-B inhibits endoplasmic reticulum-associated degradation of a misfolded α1-antitrypsin variant. FEBS J. 280, 1563-1575 (2013).
    • (2013) FEBS J. , vol.280 , pp. 1563-1575
    • Fujimori, T.1    Kamiya, Y.2    Nagata, K.3    Kato, K.4    Hosokawa, N.5
  • 64
    • 77949893248 scopus 로고    scopus 로고
    • Human XTP3-B binds to α1-antitrypsin variant null (Hong Kong) via the C-terminal MRH domain in a glycan-dependent manner
    • Yamaguchi, D., Hu, D., Matsumoto, N. & Yamamoto, K. Human XTP3-B binds to α1-antitrypsin variant null (Hong Kong) via the C-terminal MRH domain in a glycan-dependent manner. Glycobiology 20, 348-355 (2010).
    • (2010) Glycobiology , vol.20 , pp. 348-355
    • Yamaguchi, D.1    Hu, D.2    Matsumoto, N.3    Yamamoto, K.4
  • 65
    • 40249088336 scopus 로고    scopus 로고
    • OS-9 and GRP94 deliver mutant α1-antitrypsin to the Hrd1-SEL1L ubiquitin ligase complex for ERAD
    • Christianson, J. C., Shaler, T. A., Tyler, R. E. & Kopito, R. R. OS-9 and GRP94 deliver mutant α1-antitrypsin to the Hrd1-SEL1L ubiquitin ligase complex for ERAD. Nat. Cell Biol. 10, 272-282 (2008). A tour-de-force analysis of the interactome for ERAD machinery complexes.
    • (2008) Nat. Cell Biol. , vol.10 , pp. 272-282
    • Christianson, J.C.1    Shaler, T.A.2    Tyler, R.E.3    Kopito, R.R.4
  • 66
    • 80054828840 scopus 로고    scopus 로고
    • Role of the endoplasmic reticulum-associated degradation (ERAD) pathway in degradation of hepatitis C virus envelope proteins and production of virus particles
    • Saeed, M. et al. Role of the endoplasmic reticulum-associated degradation (ERAD) pathway in degradation of hepatitis C virus envelope proteins and production of virus particles. J. Biol. Chem. 286, 37264-37273 (2011).
    • (2011) J. Biol. Chem. , vol.286 , pp. 37264-37273
    • Saeed, M.1
  • 67
    • 66449136067 scopus 로고    scopus 로고
    • EDEM1 recognition and delivery of misfolded proteins to the SEL1L-containing ERAD complex
    • Cormier, J. H., Tamura, T., Sunryd, J. C. & Hebert, D. N. EDEM1 recognition and delivery of misfolded proteins to the SEL1L-containing ERAD complex. Mol. Cell 34, 627-633 (2009).
    • (2009) Mol. Cell , vol.34 , pp. 627-633
    • Cormier, J.H.1    Tamura, T.2    Sunryd, J.C.3    Hebert, D.N.4
  • 68
    • 48249117110 scopus 로고    scopus 로고
    • ERdj5 is required as a disulfide reductase for degradation of misfolded proteins in the ER
    • Ushioda, R. et al. ERdj5 is required as a disulfide reductase for degradation of misfolded proteins in the ER. Science 321, 569-572 (2008).
    • (2008) Science , vol.321 , pp. 569-572
    • Ushioda, R.1
  • 69
    • 33745893809 scopus 로고    scopus 로고
    • Decay of endoplasmic reticulum-localized mRNAs during the unfolded protein response
    • Hollien, J. & Weissman, J. S. Decay of endoplasmic reticulum-localized mRNAs during the unfolded protein response. Science 313, 104-107 (2006).
    • (2006) Science , vol.313 , pp. 104-107
    • Hollien, J.1    Weissman, J.S.2
  • 70
    • 71949098172 scopus 로고    scopus 로고
    • Signalling pathways in the unfolded protein response: Development from yeast to mammals
    • Mori, K. Signalling pathways in the unfolded protein response: development from yeast to mammals. J. Biochem. 146, 743-750 (2009).
    • (2009) J. Biochem. , vol.146 , pp. 743-750
    • Mori, K.1
  • 71
    • 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. & Wiseman, R. L. 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).
    • (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
  • 72
    • 84876991539 scopus 로고    scopus 로고
    • Stress-independent activation of XBP1s and/or ATF6 reveals three functionally diverse ER proteostasis environments
    • Shoulders, M. D. et al. Stress-independent activation of XBP1s and/or ATF6 reveals three functionally diverse ER proteostasis environments. Cell Rep. 3, 1279-1292 (2013).
    • (2013) Cell Rep. , vol.3 , pp. 1279-1292
    • Shoulders, M.D.1
  • 73
    • 84896351253 scopus 로고    scopus 로고
    • Hexosamine pathway metabolites enhance protein quality control and prolong life
    • Denzel, M. S. et al. Hexosamine pathway metabolites enhance protein quality control and prolong life. Cell 156, 1167-1178 (2014).
    • (2014) Cell , vol.156 , pp. 1167-1178
    • Denzel, M.S.1
  • 74
    • 79954423426 scopus 로고    scopus 로고
    • ERAD and ERAD tuning: Disposal of cargo and of ERAD regulators from the mammalian ER
    • Bernasconi, R. & Molinari, M. ERAD and ERAD tuning: disposal of cargo and of ERAD regulators from the mammalian ER. Curr. Opin. Cell Biol. 23, 176-183 (2011).
    • (2011) Curr. Opin. Cell Biol. , vol.23 , pp. 176-183
    • Bernasconi, R.1    Molinari, M.2
  • 75
    • 0036776098 scopus 로고    scopus 로고
    • Structural organization of the endoplasmic reticulum
    • Voeltz, G. K., Rolls, M. M. & Rapoport, T. A. Structural organization of the endoplasmic reticulum. EMBO Rep. 3, 944-950 (2002).
    • (2002) EMBO Rep. , vol.3 , pp. 944-950
    • Voeltz, G.K.1    Rolls, M.M.2    Rapoport, T.A.3
  • 76
    • 0033168581 scopus 로고    scopus 로고
    • Phosphorylation by CK2 and MAPK enhances calnexin association with ribosomes
    • Chevet, E. et al. Phosphorylation by CK2 and MAPK enhances calnexin association with ribosomes. EMBO J. 18, 3655-3666 (1999).
    • (1999) EMBO J. , vol.18 , pp. 3655-3666
    • Chevet, E.1
  • 77
    • 84883283648 scopus 로고    scopus 로고
    • Palmitoylation is the switch that assigns calnexin to quality control or ER calcium signaling
    • Lynes, E. M. et al. Palmitoylation is the switch that assigns calnexin to quality control or ER calcium signaling. J. Cell Sci. 126, 3893-3903 (2013).
    • (2013) J. Cell Sci. , vol.126 , pp. 3893-3903
    • Lynes, E.M.1
  • 78
    • 33750340637 scopus 로고    scopus 로고
    • Potent lectin-independent chaperone function of calnexin under conditions prevalent within the lumen of the endoplasmic reticulum
    • Brockmeier, A. & Williams, D. B. Potent lectin-independent chaperone function of calnexin under conditions prevalent within the lumen of the endoplasmic reticulum. Biochemistry 45, 12906-12916 (2006).
    • (2006) Biochemistry , vol.45 , pp. 12906-12916
    • Brockmeier, A.1    Williams, D.B.2
  • 79
    • 0035845484 scopus 로고    scopus 로고
    • Immunolocalization of UDP-glucose: Glycoprotein glucosyltransferase indicates involvement of pre-Golgi intermediates in protein quality control
    • Zuber, C. et al. Immunolocalization of UDP-glucose: glycoprotein glucosyltransferase indicates involvement of pre-Golgi intermediates in protein quality control. Proc. Natl. Acad. Sci. USA 98, 10710-10715 (2001).
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 10710-10715
    • Zuber, C.1
  • 80
    • 42449144739 scopus 로고    scopus 로고
    • A cell-based reglucosylation assay demonstrates the role of GT1 in the quality control of a maturing glycoprotein
    • Pearse, B. R., Gabriel, L., Wang, N. & Hebert, D. N. A cell-based reglucosylation assay demonstrates the role of GT1 in the quality control of a maturing glycoprotein. J. Cell Biol. 181, 309-320 (2008).
    • (2008) J. Cell Biol. , vol.181 , pp. 309-320
    • Pearse, B.R.1    Gabriel, L.2    Wang, N.3    Hebert, D.N.4
  • 81
    • 2342505236 scopus 로고    scopus 로고
    • Separate roles and different routing of calnexin and ERp57 in endoplasmic reticulum quality control revealed by interactions with asialoglycoprotein receptor chains
    • Frenkel, Z., Shenkman, M., Kondratyev, M. & Lederkremer, G. Z. Separate roles and different routing of calnexin and ERp57 in endoplasmic reticulum quality control revealed by interactions with asialoglycoprotein receptor chains. Mol. Biol. Cell 15, 2133-2142 (2004).
    • (2004) Mol. Biol. Cell , vol.15 , pp. 2133-2142
    • Frenkel, Z.1    Shenkman, M.2    Kondratyev, M.3    Lederkremer, G.Z.4
  • 82
    • 84890372480 scopus 로고    scopus 로고
    • Somatic mutations of calreticulin in myeloproliferative neoplasms
    • Klampfl, T. et al. Somatic mutations of calreticulin in myeloproliferative neoplasms. N. Engl. J. Med. 369, 2379-2390 (2013).
    • (2013) N. Engl. J. Med. , vol.369 , pp. 2379-2390
    • Klampfl, T.1
  • 83
    • 84892754407 scopus 로고    scopus 로고
    • Emerging principles for the therapeutic exploitation of glycosylation
    • Dalziel, M., Crispin, M., Scanlan, C. N., Zitzmann, N. & Dwek, R. A. Emerging principles for the therapeutic exploitation of glycosylation. Science 343, 1235681 (2014).
    • (2014) Science , vol.343 , pp. 1235681
    • Dalziel, M.1    Crispin, M.2    Scanlan, C.N.3    Zitzmann, N.4    Dwek, R.A.5
  • 84
    • 84874639752 scopus 로고    scopus 로고
    • An iminosugar with potent inhibition of dengue virus infection in vivo
    • Perry, S. T. et al. An iminosugar with potent inhibition of dengue virus infection in vivo. Antiviral Res. 98, 35-43 (2013).
    • (2013) Antiviral Res. , vol.98 , pp. 35-43
    • Perry, S.T.1
  • 85
    • 27244456033 scopus 로고    scopus 로고
    • Imino sugar inhibitors for treating the lysosomal glycosphingolipidoses
    • Butters, T. D., Dwek, R. A. & Platt, F. M. Imino sugar inhibitors for treating the lysosomal glycosphingolipidoses. Glycobiology 15, 43R-52R (2005).
    • (2005) Glycobiology , vol.15 , pp. 43R-52R
    • Butters, T.D.1    Dwek, R.A.2    Platt, F.M.3
  • 86
  • 87
    • 0024454546 scopus 로고
    • Perturbation of cellular calcium induces secretion of luminal ER proteins
    • Booth, C. & Koch, G. L. Perturbation of cellular calcium induces secretion of luminal ER proteins. Cell 59, 729-737 (1989).
    • (1989) Cell , vol.59 , pp. 729-737
    • Booth, C.1    Koch, G.L.2
  • 88
    • 0036115199 scopus 로고    scopus 로고
    • Calcium-pump inhibitors induce functional surface expression of ΔF508-CFTR protein in cystic fibrosis epithelial cells
    • Egan, M. E. et al. Calcium-pump inhibitors induce functional surface expression of ΔF508-CFTR protein in cystic fibrosis epithelial cells. Nat. Med. 8, 485-492 (2002).
    • (2002) Nat. Med. , vol.8 , pp. 485-492
    • Egan, M.E.1
  • 89
    • 73249114731 scopus 로고    scopus 로고
    • Rescue of CF airway epithelial cell function in vitro by a CFTR potentiator, VX-770
    • Van Goor, F. et al. Rescue of CF airway epithelial cell function in vitro by a CFTR potentiator, VX-770. Proc. Natl. Acad. Sci. USA 106, 18825-18830 (2009).
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 18825-18830
    • Van Goor, F.1
  • 90
    • 84879000844 scopus 로고    scopus 로고
    • Cystic fibrosis transmembrane regulator correctors and potentiators
    • Rowe, S. M. & Verkman, A. S. Cystic fibrosis transmembrane regulator correctors and potentiators. Cold Spring Harb. Perspect. Biol. 3, 1-15 (2013).
    • (2013) Cold Spring Harb. Perspect. Biol. , vol.3 , pp. 1-15
    • Rowe, S.M.1    Verkman, A.S.2
  • 91
    • 84863509037 scopus 로고    scopus 로고
    • Emergent properties of proteostasis in managing cystic fibrosis
    • Balch, W. E., Roth, D. M. & Hutt, D. M. Emergent properties of proteostasis in managing cystic fibrosis. Cold Spring Harb. Perspect. Biol. 3, a004499 (2011).
    • (2011) Cold Spring Harb. Perspect. Biol. , vol.3 , pp. a004499
    • Balch, W.E.1    Roth, D.M.2    Hutt, D.M.3
  • 92
    • 40149095757 scopus 로고    scopus 로고
    • Partial restoration of mutant enzyme homeostasis in three distinct lysosomal storage disease cell lines by altering calcium homeostasis
    • Mu, T. W., Fowler, D. M. & Kelly, J. W. Partial restoration of mutant enzyme homeostasis in three distinct lysosomal storage disease cell lines by altering calcium homeostasis. PLoS Biol. 6, e26 (2008).
    • (2008) PLoS Biol. , vol.6 , pp. e26
    • Mu, T.W.1    Fowler, D.M.2    Kelly, J.W.3
  • 93
    • 50249175120 scopus 로고    scopus 로고
    • Chemical and biological approaches synergize to ameliorate protein-folding diseases
    • Mu, T. W. et al. Chemical and biological approaches synergize to ameliorate protein-folding diseases. Cell 134, 769-781 (2008). Provides a powerful example of the potential utility for proteostasis regulators.
    • (2008) Cell , vol.134 , pp. 769-781
    • Mu, T.W.1
  • 95
    • 84875434910 scopus 로고    scopus 로고
    • FKBP10 depletion enhances glucocerebrosidase proteostasis in Gaucher disease fibroblasts
    • Ong, D. S. et al. FKBP10 depletion enhances glucocerebrosidase proteostasis in Gaucher disease fibroblasts. Chem. Biol. 20, 403-415 (2013).
    • (2013) Chem. Biol. , vol.20 , pp. 403-415
    • Ong, D.S.1
  • 96
    • 84868334619 scopus 로고    scopus 로고
    • Histone deacetylase inhibitor (HDACi) suberoylanilide hydroxamic acid (SAHA)-mediated correction of α1-antitrypsin deficiency
    • Bouchecareilh, M., Hutt, D. M., Szajner, P., Flotte, T. R. & Balch, W. E. Histone deacetylase inhibitor (HDACi) suberoylanilide hydroxamic acid (SAHA)-mediated correction of α1-antitrypsin deficiency. J. Biol. Chem. 287, 38265-38278 (2012).
    • (2012) J. Biol. Chem. , vol.287 , pp. 38265-38278
    • Bouchecareilh, M.1    Hutt, D.M.2    Szajner, P.3    Flotte, T.R.4    Balch, W.E.5
  • 97
    • 84890858016 scopus 로고    scopus 로고
    • SAHA enhances proteostasis of epilepsy-associated α1 (A322D) β2γ2 GABA (A) receptors
    • Di, X. J., Han, D. Y., Wang, Y. J., Chance, M. R. & Mu, T. W. SAHA enhances proteostasis of epilepsy-associated α1 (A322D) β2γ2 GABA (A) receptors. Chem. Biol. 20, 1456-1468 (2013).
    • (2013) Chem. Biol. , vol.20 , pp. 1456-1468
    • Di, X.J.1    Han, D.Y.2    Wang, Y.J.3    Chance, M.R.4    Mu, T.W.5
  • 98
    • 69449094891 scopus 로고    scopus 로고
    • Darwinian selection for sites of Asn-linked glycosylation in phylogenetically disparate eukaryotes and viruses
    • Cui, J., Smith, T., Robbins, P. W. & Samuelson, J. Darwinian selection for sites of Asn-linked glycosylation in phylogenetically disparate eukaryotes and viruses. Proc. Natl. Acad. Sci. USA 106, 13421-13426 (2009).
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 13421-13426
    • Cui, J.1    Smith, T.2    Robbins, P.W.3    Samuelson, J.4
  • 99
    • 34547409781 scopus 로고    scopus 로고
    • The evolution of N-glycan-dependent endoplasmic reticulum quality control factors for glycoprotein folding and degradation
    • Banerjee, S. et al. The evolution of N-glycan-dependent endoplasmic reticulum quality control factors for glycoprotein folding and degradation. Proc. Natl. Acad. Sci. USA 104, 11676-11681 (2007).
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 11676-11681
    • Banerjee, S.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.