메뉴 건너뛰기




Volumn 8, Issue 5, 1998, Pages 587-592

Lectins as chaperones in glycoprotein folding

Author keywords

[No Author keywords available]

Indexed keywords

CALNEXIN; CALRETICULIN; CHAPERONE; GLUCOSIDASE; GLYCOPROTEIN; LECTIN; OLIGOSACCHARIDE;

EID: 0031733824     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-440X(98)80148-6     Document Type: Article
Times cited : (216)

References (48)
  • 1
    • 0028198111 scopus 로고
    • How N-linked oligosaccharides affect glycoprotein folding in the endoplasmic reticulum
    • Helenius A. 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
  • 6
    • 0032502282 scopus 로고    scopus 로고
    • Oligosaccharide binding characteristics of the molecular chaperones calnexin and calreticulin
    • of special interest. This study, together with [7,8], demonstrates the carbohydrate binding properties of calnexin and calreticulin, and their selectivity for monoglucosylated oligosaccharides.
    • Vassilakos A, Michalak M, Lehrman M, Williams DB. Oligosaccharide binding characteristics of the molecular chaperones calnexin and calreticulin. of special interest Biochemistry. 37:1998;3480-3490 This study, together with [7,8], demonstrates the carbohydrate binding properties of calnexin and calreticulin, and their selectivity for monoglucosylated oligosaccharides.
    • (1998) Biochemistry , vol.37 , pp. 3480-3490
    • Vassilakos, A.1    Michalak, M.2    Lehrman, M.3    Williams, D.B.4
  • 8
    • 15844386822 scopus 로고    scopus 로고
    • Definition of the lectin-like properties of the molecular chaperone, calreticulin, and demonstration of its copurification with endomannosidase from rat liver Golgi
    • Spiro RG, Zhu Q, Bhoyroo V, Soling HD. Definition of the lectin-like properties of the molecular chaperone, calreticulin, and demonstration of its copurification with endomannosidase from rat liver Golgi. J Biol Chem. 271:1996;11588-11594.
    • (1996) J Biol Chem , vol.271 , pp. 11588-11594
    • Spiro, R.G.1    Zhu, Q.2    Bhoyroo, V.3    Soling, H.D.4
  • 9
    • 0020957538 scopus 로고
    • 2 in calf thyroid cells. A possible recognition signal in the processing of glycoproteins
    • 2 in calf thyroid cells. A possible recognition signal in the processing of glycoproteins. J Biol Chem. 258:1983;8260-8265.
    • (1983) J Biol Chem , vol.258 , pp. 8260-8265
    • Parodi, A.J.1    Mendelzon, D.H.2    Lederkremer, G.H.3
  • 10
    • 0030839727 scopus 로고    scopus 로고
    • The solution NMR structure of glucosylated N-glycans involved in the early stages of glycoprotein biosynthesis and folding
    • Petrescu AJ, Butters TD, Reinkensmeier G, Petrescu S, Platt FM, Dwek RA, Wormald MR. The solution NMR structure of glucosylated N-glycans involved in the early stages of glycoprotein biosynthesis and folding. EMBO J. 16:1997;4302-4310.
    • (1997) EMBO J , vol.16 , pp. 4302-4310
    • Petrescu, A.J.1    Butters, T.D.2    Reinkensmeier, G.3    Petrescu, S.4    Platt, F.M.5    Dwek, R.A.6    Wormald, M.R.7
  • 11
    • 15844379984 scopus 로고    scopus 로고
    • Glycan dependent and independent association of vesicular stomatitis virus G protein with calnexin
    • Cannon KS, Hebert DN, Helenius A. Glycan dependent and independent association of vesicular stomatitis virus G protein with calnexin. J Biol Chem. 271:1996;14280-14284.
    • (1996) J Biol Chem , vol.271 , pp. 14280-14284
    • Cannon, K.S.1    Hebert, D.N.2    Helenius, A.3
  • 12
    • 0030449989 scopus 로고    scopus 로고
    • N-linked oligosaccharides are necessary and sufficient for association of glycosylated forms of bovine RNase with calnexin and calreticulin
    • Rodan AR, Simons JF, Trombetta ES, Helenius A. N-linked oligosaccharides are necessary and sufficient for association of glycosylated forms of bovine RNase with calnexin and calreticulin. EMBO J. 15:1996;6921-6930.
    • (1996) EMBO J , vol.15 , pp. 6921-6930
    • Rodan, A.R.1    Simons, J.F.2    Trombetta, E.S.3    Helenius, A.4
  • 13
    • 0031045007 scopus 로고    scopus 로고
    • Interactions between newly synthesized glycoproteins, calnexin and a network of resident chaperones in the endoplasmic reticulum
    • Tatu U, Helenius A. Interactions between newly synthesized glycoproteins, calnexin and a network of resident chaperones in the endoplasmic reticulum. J Cell Biol. 136:1997;555-565.
    • (1997) J Cell Biol , vol.136 , pp. 555-565
    • Tatu, U.1    Helenius, A.2
  • 14
    • 0032478644 scopus 로고    scopus 로고
    • Differential interaction of coagulation factor VIII and factor V with protein chaperones calnexin and calreticulin
    • Pipe SW, Morris JA, Shah J, Kaufman RJ. Differential interaction of coagulation factor VIII and factor V with protein chaperones calnexin and calreticulin. J Biol Chem. 273:1998;8537-8544.
    • (1998) J Biol Chem , vol.273 , pp. 8537-8544
    • Pipe, S.W.1    Morris, J.A.2    Shah, J.3    Kaufman, R.J.4
  • 15
    • 0031895637 scopus 로고    scopus 로고
    • Mechanism of MHC class I-restricted antigen processing
    • Pamer E, Cresswell P. Mechanism of MHC class I-restricted antigen processing. Annu Rev Immunol. 16:1998;323-358.
    • (1998) Annu Rev Immunol , vol.16 , pp. 323-358
    • Pamer, E.1    Cresswell, P.2
  • 16
    • 0032522392 scopus 로고    scopus 로고
    • ER-60, a chaperone with thiol-dependent reductase activity involved in MHC class I assembly
    • Lindquist JA, Jensen ON, Mann M, Hammerling GJ. ER-60, a chaperone with thiol-dependent reductase activity involved in MHC class I assembly. EMBO J. 17:1998;2186-2195.
    • (1998) EMBO J , vol.17 , pp. 2186-2195
    • Lindquist, J.A.1    Jensen, O.N.2    Mann, M.3    Hammerling, G.J.4
  • 17
    • 0029024748 scopus 로고
    • Glucose trimming and reglucosylation determine glycoprotein association with calnexin in the endoplasmic reticulum
    • Hebert DN, Foellmer B, Helenius A. Glucose trimming and reglucosylation determine glycoprotein association with calnexin in the endoplasmic reticulum. Cell. 81:1995;425-433.
    • (1995) Cell , vol.81 , pp. 425-433
    • Hebert, D.N.1    Foellmer, B.2    Helenius, A.3
  • 18
    • 0029934119 scopus 로고    scopus 로고
    • Calnexin and calreticulin promote folding, delay oligomerization and suppress degradation of influenza hemagglutinin in microsomes
    • Hebert DN, Foellmer B, Helenius A. Calnexin and calreticulin promote folding, delay oligomerization and suppress degradation of influenza hemagglutinin in microsomes. EMBO J. 15:1996;2961-2968.
    • (1996) EMBO J , vol.15 , pp. 2961-2968
    • Hebert, D.N.1    Foellmer, B.2    Helenius, A.3
  • 19
    • 0030467255 scopus 로고    scopus 로고
    • Deglucosylation of N-linked glycans is an important step in the dissociation of calreticulin-class I-TAP complexes
    • van Leeuwn JEM, Kearse KP. Deglucosylation of N-linked glycans is an important step in the dissociation of calreticulin-class I-TAP complexes. Proc Natl Acad Sci USA. 93:1996;13997-14001.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 13997-14001
    • Van Leeuwn, J.E.M.1    Kearse, K.P.2
  • 20
    • 0030815129 scopus 로고    scopus 로고
    • Promotion of transferrin folding by cyclic interactions with calnexin and calreticulin
    • Wada I, Kai M, Imai S, Sakane F, Kanoh H. Promotion of transferrin folding by cyclic interactions with calnexin and calreticulin. EMBO J. 16:1997;5420-5432.
    • (1997) EMBO J , vol.16 , pp. 5420-5432
    • Wada, I.1    Kai, M.2    Imai, S.3    Sakane, F.4    Kanoh, H.5
  • 21
    • 0028103695 scopus 로고
    • Role of N-linked oligosaccharide recognition, glucose trimming, and calnexin in glycoprotein folding and quality control
    • Hammond C, Braakman I, Helenius A. Role of N-linked oligosaccharide recognition, glucose trimming, and calnexin in glycoprotein folding and quality control. Proc Natl Acad Sci USA. 91:1994;913-917.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 913-917
    • Hammond, C.1    Braakman, I.2    Helenius, A.3
  • 22
    • 0026799435 scopus 로고
    • Purification to apparent homogeneity and partial characterization of rat liver UDP-glucose:glycoprotein glucosyltransferase
    • Trombetta SE, Parodi AJ. Purification to apparent homogeneity and partial characterization of rat liver UDP-glucose:glycoprotein glucosyltransferase. J Biol Chem. 267:1992;9236-9240.
    • (1992) J Biol Chem , vol.267 , pp. 9236-9240
    • Trombetta, S.E.1    Parodi, A.J.2
  • 23
    • 0026500202 scopus 로고
    • Recognition of the oligosaccharide and protein moieties of glycoproteins by the UDP-Glc:glycoprotein glucosyltransferase
    • Sousa MC, Ferrero GM, Parodi AJ. Recognition of the oligosaccharide and protein moieties of glycoproteins by the UDP-Glc:glycoprotein glucosyltransferase. Biochemistry. 31:1992;97-105.
    • (1992) Biochemistry , vol.31 , pp. 97-105
    • Sousa, M.C.1    Ferrero, G.M.2    Parodi, A.J.3
  • 24
  • 25
    • 0031041169 scopus 로고    scopus 로고
    • Reglucosylation of N-linked glycans is critical for calnexin assembly with T cell receptor (TCR) alpha proteins but not TCR beta proteins
    • van Leeuwn LEM, Kearse KP. Reglucosylation of N-linked glycans is critical for calnexin assembly with T cell receptor (TCR) alpha proteins but not TCR beta proteins. J Biol Chem. 272:1997;4179-4186.
    • (1997) J Biol Chem , vol.272 , pp. 4179-4186
    • Van Leeuwn, L.E.M.1    Kearse, K.P.2
  • 26
    • 0024598083 scopus 로고
    • Selective retention of monoglucosylated high mannose oligosaccharides by a class of mutant vesicular stomatitis virus G proteins
    • Suh K, Bergmann JE, Gabel CA. Selective retention of monoglucosylated high mannose oligosaccharides by a class of mutant vesicular stomatitis virus G proteins. J Cell Biol. 108:1989;811-819.
    • (1989) J Cell Biol , vol.108 , pp. 811-819
    • Suh, K.1    Bergmann, J.E.2    Gabel, C.A.3
  • 27
    • 0028076031 scopus 로고
    • Folding of VSV G protein: Sequential interaction with BiP and calnexin
    • Hammond C, Helenius A. Folding of VSV G protein: sequential interaction with BiP and calnexin. Science. 266:1994;456-458.
    • (1994) Science , vol.266 , pp. 456-458
    • Hammond, C.1    Helenius, A.2
  • 28
    • 0028965533 scopus 로고
    • Molecular chaperones in antigen presentation
    • Williams DB, Watts TH. Molecular chaperones in antigen presentation. Curr Opin Immunol. 7:1995;77-84.
    • (1995) Curr Opin Immunol , vol.7 , pp. 77-84
    • Williams, D.B.1    Watts, T.H.2
  • 29
    • 0032101943 scopus 로고    scopus 로고
    • Calreticulin and calnexin interact with different protein and glycan determinants during the assembly of MHC class I
    • Harris MR, Yu YY, Kindle CS, Hansen L, Solheim TH. Calreticulin and calnexin interact with different protein and glycan determinants during the assembly of MHC class I. J Immunol. 160:1998;5404-5409.
    • (1998) J Immunol , vol.160 , pp. 5404-5409
    • Harris, M.R.1    Yu, Y.Y.2    Kindle, C.S.3    Hansen, L.4    Solheim, T.H.5
  • 30
    • 0030667061 scopus 로고    scopus 로고
    • The number and location of glycans on influenza hemagglutinin determine folding and association with calnexin and calreticulin
    • of special interest. This study explores the determinants for the selective binding by calnexin and calreticulin, suggesting how folding status, linked to the location of the oligosaccharides, can favor interaction with either chaperone.
    • Hebert DN, Zhang JX, Chen W, Foellmer B, Helenius A. The number and location of glycans on influenza hemagglutinin determine folding and association with calnexin and calreticulin. of special interest J Cell Biol. 139:1997;613-623 This study explores the determinants for the selective binding by calnexin and calreticulin, suggesting how folding status, linked to the location of the oligosaccharides, can favor interaction with either chaperone.
    • (1997) J Cell Biol , vol.139 , pp. 613-623
    • Hebert, D.N.1    Zhang, J.X.2    Chen, W.3    Foellmer, B.4    Helenius, A.5
  • 31
    • 0030912157 scopus 로고    scopus 로고
    • Aberrant retention of tyrosinase in the endoplasmic reticulum mediates accelerated degradation of the enzyme and contributes to the dedifferentiated phenotype of amelanotic melanoma cells
    • Halaban R, Cheng E, Zhang Y, Moellmann G, Hanlon D, Michalak M, Setaluri V, Hebert DN. Aberrant retention of tyrosinase in the endoplasmic reticulum mediates accelerated degradation of the enzyme and contributes to the dedifferentiated phenotype of amelanotic melanoma cells. Proc Natl Acad Sci USA. 94:1997;6210-6215.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 6210-6215
    • Halaban, R.1    Cheng, E.2    Zhang, Y.3    Moellmann, G.4    Hanlon, D.5    Michalak, M.6    Setaluri, V.7    Hebert, D.N.8
  • 32
    • 0031035644 scopus 로고    scopus 로고
    • Interaction of the thiol dependent reductase ERp57 with nascent glycoproteins
    • of outstanding interest. This study shows, for the first time, the interaction of ERp57 with partially deglucosylated glycoproteins. A number of studies then followed, establishing ERp57 as a component of the glycoprotein-specific quality control machinery in the ER.
    • Oliver JD, van der Wal FJ, Bulleid NJ, High S. Interaction of the thiol dependent reductase ERp57 with nascent glycoproteins. of outstanding interest Science. 275:1997;86-88 This study shows, for the first time, the interaction of ERp57 with partially deglucosylated glycoproteins. A number of studies then followed, establishing ERp57 as a component of the glycoprotein-specific quality control machinery in the ER.
    • (1997) Science , vol.275 , pp. 86-88
    • Oliver, J.D.1    Van Der Wal, F.J.2    Bulleid, N.J.3    High, S.4
  • 33
    • 0030960372 scopus 로고    scopus 로고
    • The thiol-dependent reductase ERp57 interacts specifically with N-glycosylated integral membrane proteins
    • Elliott JG, Oliver JD, High S. The thiol-dependent reductase ERp57 interacts specifically with N-glycosylated integral membrane proteins. J Biol Chem. 272:1997;13849-13855.
    • (1997) J Biol Chem , vol.272 , pp. 13849-13855
    • Elliott, J.G.1    Oliver, J.D.2    High, S.3
  • 34
    • 0032513212 scopus 로고
    • Enhanced catalysis of ribonuclease B folding by the interaction of calnexin or calreticulin with ERp57
    • Zapun A, Darby NJ, Tessier DC, Michalak M, Bergeron JJ, Thomas DY. Enhanced catalysis of ribonuclease B folding by the interaction of calnexin or calreticulin with ERp57. J Biol Chem. 273:1988;6009-6012.
    • (1988) J Biol Chem , vol.273 , pp. 6009-6012
    • Zapun, A.1    Darby, N.J.2    Tessier, D.C.3    Michalak, M.4    Bergeron, J.J.5    Thomas, D.Y.6
  • 35
    • 0029925940 scopus 로고    scopus 로고
    • The molecular chaperone calnexin facilitates folding and assembly of class I histocompatibility molecules
    • Vassilakos A, Cohen DM, Peterson PA, Jackson MR, Williams DB. The molecular chaperone calnexin facilitates folding and assembly of class I histocompatibility molecules. EMBO J. 15:1996;1495-1506.
    • (1996) EMBO J , vol.15 , pp. 1495-1506
    • Vassilakos, A.1    Cohen, D.M.2    Peterson, P.A.3    Jackson, M.R.4    Williams, D.B.5
  • 36
    • 0032482220 scopus 로고    scopus 로고
    • Folding of insulin receptor monomers is facilitated by the molecular chaperones calnexin and calreticulin and impaired by rapid dimerization
    • Bass J, Chiu G, Argon Y, Steiner DF. Folding of insulin receptor monomers is facilitated by the molecular chaperones calnexin and calreticulin and impaired by rapid dimerization. J Cell Biol. 141:1998;637-646.
    • (1998) J Cell Biol , vol.141 , pp. 637-646
    • Bass, J.1    Chiu, G.2    Argon, Y.3    Steiner, D.F.4
  • 37
    • 0030881717 scopus 로고    scopus 로고
    • Quality control in the secretory pathway: The role of calreticulin, calnexin and BiP in the retention of glycoproteins with C-terminal truncations
    • Zhang JX, Braakman I, Matlack KE, Helenius A. Quality control in the secretory pathway: the role of calreticulin, calnexin and BiP in the retention of glycoproteins with C-terminal truncations. Mol Biol Cell. 8:1997;1943-1954.
    • (1997) Mol Biol Cell , vol.8 , pp. 1943-1954
    • Zhang, J.X.1    Braakman, I.2    Matlack, K.E.3    Helenius, A.4
  • 38
    • 0032521621 scopus 로고
    • In vitro characterisation of the interaction between newly synthesized proteins and a pancreatic isoform of protein disulfide isomerase
    • Elliott JG, Oliver JD, Volkmer H, Zimmerman R, High S. In vitro characterisation of the interaction between newly synthesized proteins and a pancreatic isoform of protein disulfide isomerase. Eur J Biochem. 252:1988;372-377.
    • (1988) Eur J Biochem , vol.252 , pp. 372-377
    • Elliott, J.G.1    Oliver, J.D.2    Volkmer, H.3    Zimmerman, R.4    High, S.5
  • 39
    • 0028339518 scopus 로고
    • Quality control in the secretory pathway: Retention of a misfolded viral membrane glycoprotein involves cycling between the ER, intermediate compartment, and Golgi apparatus
    • Hammond C, Helenius A. Quality control in the secretory pathway: retention of a misfolded viral membrane glycoprotein involves cycling between the ER, intermediate compartment, and Golgi apparatus. J Cell Biol. 126:1994;41-52.
    • (1994) J Cell Biol , vol.126 , pp. 41-52
    • Hammond, C.1    Helenius, A.2
  • 42
    • 0029819131 scopus 로고    scopus 로고
    • N-butyldeoxynojirimycin-mediated inhibition of human immunodeficiency virus entry correlates with changes in antibody recognition of the V1/V2 region of gp120
    • Fischer PB, Karlsson GB, Butters TD, Dwek RA, Platt FM. N-butyldeoxynojirimycin-mediated inhibition of human immunodeficiency virus entry correlates with changes in antibody recognition of the V1/V2 region of gp120. J Virol. 70:1996;7143-7152.
    • (1996) J Virol , vol.70 , pp. 7143-7152
    • Fischer, P.B.1    Karlsson, G.B.2    Butters, T.D.3    Dwek, R.A.4    Platt, F.M.5
  • 43
    • 0031058830 scopus 로고    scopus 로고
    • Hepatitis B virus (HBV) envelope glycoproteins vary drastically in their sensitivity to glycan processing: Evidence that alteration of a single N-linked glycosylation site can regulate HBV secretion
    • Mehta A, Lu X, Block TM, Blumberg BS, Dwek RA. Hepatitis B virus (HBV) envelope glycoproteins vary drastically in their sensitivity to glycan processing: evidence that alteration of a single N-linked glycosylation site can regulate HBV secretion. Proc Natl Acad Sci USA. 94:1997;1822-1827.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 1822-1827
    • Mehta, A.1    Lu, X.2    Block, T.M.3    Blumberg, B.S.4    Dwek, R.A.5
  • 44
    • 0030948755 scopus 로고    scopus 로고
    • Inhibition of N-glycan processing in B16 melanoma cells results in inactivation of tyrosinase but does not prevent its transport to the melanosome
    • Petrescu SM, Petrescu AJ, Titu HN, Dwek RA, Platt FM. Inhibition of N-glycan processing in B16 melanoma cells results in inactivation of tyrosinase but does not prevent its transport to the melanosome. J Biol Chem. 272:1997;15796-15803.
    • (1997) J Biol Chem , vol.272 , pp. 15796-15803
    • Petrescu, S.M.1    Petrescu, A.J.2    Titu, H.N.3    Dwek, R.A.4    Platt, F.M.5
  • 46
    • 0032482384 scopus 로고    scopus 로고
    • The thiol oxidoreductase ERp57 is a component of the MHC class I peptide-loading complex
    • Hughes EA, Cresswell P. The thiol oxidoreductase ERp57 is a component of the MHC class I peptide-loading complex. Curr Biol. 4:1998;709-712.
    • (1998) Curr Biol , vol.4 , pp. 709-712
    • Hughes, E.A.1    Cresswell, P.2
  • 47
    • 0032482385 scopus 로고    scopus 로고
    • A role for the thiol-dependent reductase ERp57 in the assembly of MHC class I molecules
    • Morrice NA, Powis SJ. A role for the thiol-dependent reductase ERp57 in the assembly of MHC class I molecules. Curr Biol. 4:1998;713-716.
    • (1998) Curr Biol , vol.4 , pp. 713-716
    • Morrice, N.A.1    Powis, S.J.2
  • 48
    • 0032486274 scopus 로고    scopus 로고
    • Calnexin associates with monomeric and oligomeric (disulfide-linked) CD3 delta proteins in murine T lymphocytes
    • Kearse KP. Calnexin associates with monomeric and oligomeric (disulfide-linked) CD3 delta proteins in murine T lymphocytes. J Biol Chem. 273:1998;14152-14157.
    • (1998) J Biol Chem , vol.273 , pp. 14152-14157
    • Kearse, K.P.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.