메뉴 건너뛰기




Volumn 88, Issue 1, 1997, Pages 29-38

Conformation-independent binding of monoglucosylated ribonuclease B to calnexin

Author keywords

[No Author keywords available]

Indexed keywords

CALNEXIN; GLUCOSIDASE; GLUCOSYLTRANSFERASE; OLIGOSACCHARIDE; PROTEIN DISULFIDE ISOMERASE; RIBONUCLEASE; URIDINE DIPHOSPHATE GLUCOSE;

EID: 0030933129     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0092-8674(00)81855-3     Document Type: Article
Times cited : (187)

References (43)
  • 1
    • 0028888054 scopus 로고
    • Molecular requirements for the interaction of class II major histocompatibility complex molecules and invariant chain with calnexin
    • Arunachalam, B., and Cresswell, P. (1995). Molecular requirements for the interaction of class II major histocompatibility complex molecules and invariant chain with calnexin. J. Biol. Chem. 270, 2784-2790.
    • (1995) J. Biol. Chem. , vol.270 , pp. 2784-2790
    • Arunachalam, B.1    Cresswell, P.2
  • 2
    • 0028810104 scopus 로고
    • Unique expression of major histocompatibility complex class I proteins in the absence of glucose trimming and calnexin association
    • Balow, J.P., Weissman, J.D., and Kearse, K.P. (1995). Unique expression of major histocompatibility complex class I proteins in the absence of glucose trimming and calnexin association. J. Biol. Chem. 270, 29025-29029.
    • (1995) J. Biol. Chem. , vol.270 , pp. 29025-29029
    • Balow, J.P.1    Weissman, J.D.2    Kearse, K.P.3
  • 3
    • 0021245984 scopus 로고
    • Isolation of a homogeneous glucosidase II from pig kidney microsomes
    • Brada, D., and Dubach, U.C. (1984). Isolation of a homogeneous glucosidase II from pig kidney microsomes. Eur. J. Biochem. 141, 149-156.
    • (1984) Eur. J. Biochem. , vol.141 , pp. 149-156
    • Brada, D.1    Dubach, U.C.2
  • 4
    • 15844379984 scopus 로고    scopus 로고
    • Glycan dependent and independent association of vesicular stomatitis virus G protein with calnexin
    • Cannon, K.S., Hebert, D.N., and Helenius, A. (1996). Glycan dependent and independent association of vesicular stomatitis virus G protein with calnexin. J. Biol. Chem. 277, 14280-14284.
    • (1996) J. Biol. Chem. , vol.277 , pp. 14280-14284
    • Cannon, K.S.1    Hebert, D.N.2    Helenius, A.3
  • 5
    • 0029073719 scopus 로고
    • Aglycosylated and phosphatidylinositolanchored MHC class I molecules are associated with calnexin
    • Carreno, B.M., Schreiber, K.L, McKean, D.J., Stroynowski, I., and Hansen, T.H. (1995). Aglycosylated and phosphatidylinositolanchored MHC class I molecules are associated with calnexin. J. Immunol. 154, 5173-5180.
    • (1995) J. Immunol. , vol.154 , pp. 5173-5180
    • Carreno, B.M.1    Schreiber, K.L.2    McKean, D.J.3    Stroynowski, I.4    Hansen, T.H.5
  • 6
    • 0022578323 scopus 로고
    • Requirements of cleavage of high mannose oligosaccharides in glycoproteins by peptide N-glycosidase F
    • Chu, F.K. (1986). Requirements of cleavage of high mannose oligosaccharides in glycoproteins by peptide N-glycosidase F. J. Biol. Chem. 267, 172-177.
    • (1986) J. Biol. Chem. , vol.267 , pp. 172-177
    • Chu, F.K.1
  • 7
    • 0018791296 scopus 로고
    • Intermediates in the refolding of reduced ribonuclease A
    • Creighton, T.E. (1979). Intermediates in the refolding of reduced ribonuclease A. J. Mol. Biol. 129, 411-431.
    • (1979) J. Mol. Biol. , vol.129 , pp. 411-431
    • Creighton, T.E.1
  • 8
    • 0029093531 scopus 로고
    • Functional properties of the individual thioredoxin-like domains of protein disulfide isomerase
    • Darby, N.J., and Creighton, T.E. (1995). Functional properties of the individual thioredoxin-like domains of protein disulfide isomerase. Biochemistry 34, 11725-11735.
    • (1995) Biochemistry , vol.34 , pp. 11725-11735
    • Darby, N.J.1    Creighton, T.E.2
  • 9
    • 0020468220 scopus 로고
    • Inhibition of formation of complex oligosaccharides by the glucosidase inhibitor bromoconduritol
    • Datema, R., Romero, P.A., Legler, G., and Schwarz, R.T. (1982). Inhibition of formation of complex oligosaccharides by the glucosidase inhibitor bromoconduritol. Proc. Natl. Acad. Sci. USA 79, 6787-6791.
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 6787-6791
    • Datema, R.1    Romero, P.A.2    Legler, G.3    Schwarz, R.T.4
  • 10
    • 0023645327 scopus 로고
    • The mechanism of folding of pancreatic ribonucleases is independent of the presence of covalently linked carbohydrate
    • Grafl, R., Lang, K., Vogl H., and Schmid, F.X. (1987). The mechanism of folding of pancreatic ribonucleases is independent of the presence of covalently linked carbohydrate. J. Biol. Chem. 262, 10624-10629.
    • (1987) J. Biol. Chem. , vol.262 , pp. 10624-10629
    • Grafl, R.1    Lang, K.2    Vogl, H.3    Schmid, F.X.4
  • 11
    • 0019332339 scopus 로고
    • Substrate specificities of rat liver microsomal glucosidases which process glycoproteins
    • Grinna, L.S., and Robbins, P.W. (1980). Substrate specificities of rat liver microsomal glucosidases which process glycoproteins. J. Biol. Chem. 255, 2255-2258.
    • (1980) J. Biol. Chem. , vol.255 , pp. 2255-2258
    • Grinna, L.S.1    Robbins, P.W.2
  • 12
    • 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
  • 13
    • 0029024748 scopus 로고
    • Glucose trimming and reglucosylation determine glycoprotein association with calnexin in the endoplasmic reticulum
    • Hebert, D.N., Foellmer, B., and Helenius, A. (1995). Glucose trimming and reglucosylation determine glycoprotein association with calnexin in the endoplasmic reticulum. Cell 81, 425-433.
    • (1995) Cell , vol.81 , pp. 425-433
    • Hebert, D.N.1    Foellmer, B.2    Helenius, A.3
  • 14
    • 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., and Helenius, A. (1996). Calnexin and calreticulin promote folding, delay oligomerization and suppress degradation of influenza hemagglutinin in microsomes. EMBO J. 12, 2961-2968.
    • (1996) EMBO J. , vol.12 , pp. 2961-2968
    • Hebert, D.N.1    Foellmer, B.2    Helenius, A.3
  • 15
    • 0028198111 scopus 로고
    • How W-linked oligosaccharides affect glycoprotein folding in the endoplasmic reticulum
    • Helenius, A. (1994). How W-linked oligosaccharides affect glycoprotein folding in the endoplasmic reticulum. Mol. Biol. Cell 5, 253-265.
    • (1994) Mol. Biol. Cell , vol.5 , pp. 253-265
    • Helenius, A.1
  • 16
    • 0027184721 scopus 로고
    • Molecularchaperone functions of heat-shock proteins
    • Hendrick, J.P., and Hartl, F.U. (1993). Molecularchaperone functions of heat-shock proteins. Annu. Rev. Biochem. 62, 349-384.
    • (1993) Annu. Rev. Biochem. , vol.62 , pp. 349-384
    • Hendrick, J.P.1    Hartl, F.U.2
  • 17
    • 0019377631 scopus 로고
    • Synthesis and processing of asparagine-linked oligosaccharides
    • Hubbard, S.C., and Ivatt, R.J. (1981). Synthesis and processing of asparagine-linked oligosaccharides. Annu. Rev. Biochem. 50, 555-584.
    • (1981) Annu. Rev. Biochem. , vol.50 , pp. 555-584
    • Hubbard, S.C.1    Ivatt, R.J.2
  • 18
    • 0027993624 scopus 로고
    • Persistence of glucose residues on core oligosaccharides prevents association of TCRα and TCRβ proteins with calnexin and results specifically in accelerated degradation of nascent TCRα proteins within the endoplasmic reticulum
    • Kearse, K.P., Williams, D.B., and Singer, A. (1994). Persistence of glucose residues on core oligosaccharides prevents association of TCRα and TCRβ proteins with calnexin and results specifically in accelerated degradation of nascent TCRα proteins within the endoplasmic reticulum. EMBO J. 13, 3678-3686.
    • (1994) EMBO J. , vol.13 , pp. 3678-3686
    • Kearse, K.P.1    Williams, D.B.2    Singer, A.3
  • 19
    • 0028801931 scopus 로고
    • Calnexin and BiP act as sequential molecular chaperones during thyroglobulin folding in the endoplasmic reticulum
    • Kim, P., and Arvan, P. (1995). Calnexin and BiP act as sequential molecular chaperones during thyroglobulin folding in the endoplasmic reticulum. J. Cell. Biol. 128, 29-38.
    • (1995) J. Cell. Biol. , vol.128 , pp. 29-38
    • Kim, P.1    Arvan, P.2
  • 20
    • 0029099301 scopus 로고
    • P-glycoprotein, associations between domains and molecular chaperones
    • Loo, T.W., and Clarke, D.M. (1995). P-glycoprotein, associations between domains and molecular chaperones. J. Biol. Chem. 270, 21839-21844.
    • (1995) J. Biol. Chem. , vol.270 , pp. 21839-21844
    • Loo, T.W.1    Clarke, D.M.2
  • 21
    • 0025972887 scopus 로고
    • Catalysis of the oxidative folding of ribonuclease A by protein disulfide isomerase: Pre-steady-state kinetics and the utilization of the oxidizing equivalents of the isomerase
    • Lyles, M.M., and Gilbert, H.F. (1991). Catalysis of the oxidative folding of ribonuclease A by protein disulfide isomerase: pre-steady-state kinetics and the utilization of the oxidizing equivalents of the isomerase. Biochemistry 30, 619-625.
    • (1991) Biochemistry , vol.30 , pp. 619-625
    • Lyles, M.M.1    Gilbert, H.F.2
  • 22
    • 0028964421 scopus 로고
    • Calreticulin functions as a molecular chaperone in the biosynthesis of myeloperoxidase
    • Nauseef, W.M., McCormick, S.J., and Clark, R.A. (1995). Calreticulin functions as a molecular chaperone in the biosynthesis of myeloperoxidase. J. Biol. Chem. 270, 4741-4747.
    • (1995) J. Biol. Chem. , vol.270 , pp. 4741-4747
    • Nauseef, W.M.1    McCormick, S.J.2    Clark, R.A.3
  • 23
    • 0028883409 scopus 로고
    • Calnexin fails to associate with substrate proteins in glucosidase-deficient cell lines
    • Ora, A., and Helenius, A. (1995). Calnexin fails to associate with substrate proteins in glucosidase-deficient cell lines. J. Biol. Chem. 270, 26060-26062.
    • (1995) J. Biol. Chem. , vol.270 , pp. 26060-26062
    • Ora, A.1    Helenius, A.2
  • 24
    • 0027295871 scopus 로고
    • Association of folding intermediates of glycoproteins with calnexin during protein maturation
    • Ou, W.J., Cameron, P.H., Thomas, D.Y.,and Bergeron, J.J.M. (1993). Association of folding intermediates of glycoproteins with calnexin during protein maturation. Nature 364, 771-776.
    • (1993) Nature , vol.364 , pp. 771-776
    • Ou, W.J.1    Cameron, P.H.2    Thomas, D.Y.3    Bergeron, J.J.M.4
  • 27
    • 0029160540 scopus 로고
    • Transient, lectin-like association of calreticulin with folding intermediates of cellular and viral glycoproteins
    • Peterson, J., Ora, A., Van, P.M., and Helenius, A. (1995). Transient, lectin-like association of calreticulin with folding intermediates of cellular and viral glycoproteins. Mol. Biol. Cell 6, 1173-1184.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 1173-1184
    • Peterson, J.1    Ora, A.2    Van, P.M.3    Helenius, A.4
  • 28
    • 0028147528 scopus 로고
    • Retention of unassembled components of integral membrane proteins by calnexin
    • Rajagopalan, S., Xu, Y., and Brenner, M.B. (1994). Retention of unassembled components of integral membrane proteins by calnexin. Science 263, 387-390.
    • (1994) Science , vol.263 , pp. 387-390
    • Rajagopalan, S.1    Xu, Y.2    Brenner, M.B.3
  • 30
    • 0029126624 scopus 로고
    • The molecular basis for the recognition of misfolded glycoproteins by the UDP-Glc:Glycoprotein glucosyltransferase
    • Sousa, M., and Parodi, A.J. (1995). The molecular basis for the recognition of misfolded glycoproteins by the UDP-Glc:glycoprotein glucosyltransferase. EMBO J. 14, 4196-4203.
    • (1995) EMBO J. , vol.14 , pp. 4196-4203
    • Sousa, M.1    Parodi, A.J.2
  • 31
    • 0026500202 scopus 로고
    • Recognition of the oligosaccharide and protein moieties of glycoproteins by the UDP-Glc:Glycoprotein glucosyltransferase
    • Sousa, M.C., Ferrero Garcia, M.A.,and Parodi, A.J. (1992). Recognition of the oligosaccharide and protein moieties of glycoproteins by the UDP-Glc:glycoprotein glucosyltransferase. Biochemistry 31, 97-105.
    • (1992) Biochemistry , vol.31 , pp. 97-105
    • Sousa, M.C.1    Ferrero Garcia, M.A.2    Parodi, A.J.3
  • 32
    • 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, R.G., Zhu, Q., Bhoyroo, V., and Söling, H.D. (1996). 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, 11588-11594.
    • (1996) J. Biol. Chem. , vol.271 , pp. 11588-11594
    • Spiro, R.G.1    Zhu, Q.2    Bhoyroo, V.3    Söling, H.D.4
  • 33
    • 0024598083 scopus 로고
    • Selective retention of monoglucosylated high mannose oligosaccharides by a class of mutant vesicular stomatitis virus G proteins
    • Suh, K., Bergman, J.E., and Gabel, C.A. (1989). Selective retention of monoglucosylated high mannose oligosaccharides by a class of mutant vesicular stomatitis virus G proteins. J. Biol. Chem. 108, 811-819.
    • (1989) J. Biol. Chem. , vol.108 , pp. 811-819
    • Suh, K.1    Bergman, J.E.2    Gabel, C.A.3
  • 34
    • 0028906029 scopus 로고
    • Folding and oligomerization of influenza hemagglutinin in the ER and the intermediate compartment
    • Tatu, U., Hammond, C., and Helenius, A. (1995). Folding and oligomerization of influenza hemagglutinin in the ER and the intermediate compartment. EMBO J. 14, 1340-1348.
    • (1995) EMBO J. , vol.14 , pp. 1340-1348
    • Tatu, U.1    Hammond, C.2    Helenius, A.3
  • 35
    • 0024468302 scopus 로고
    • Glucosylation of glycoproteins by mammalian, plant, fungal, and trypanosomatid protozoa microsomal membranes
    • Trombetta, S.E., Bosch, M., and Parodi, A.J. (1989). Glucosylation of glycoproteins by mammalian, plant, fungal, and trypanosomatid protozoa microsomal membranes. Biochemistry 28, 8108-8116.
    • (1989) Biochemistry , vol.28 , pp. 8108-8116
    • Trombetta, S.E.1    Bosch, M.2    Parodi, A.J.3
  • 36
    • 0026799435 scopus 로고
    • Purification to apparent homogeneity and partial characterization of rat liver UDP-glucose:Glycoprotein glucosyltransferase
    • Trombetta, S.E., and Parodi, A.J. (1992). Purification to apparent homogeneity and partial characterization of rat liver UDP-glucose:glycoprotein glucosyltransferase. J. Biol. Chem. 267, 9236-9240.
    • (1992) J. Biol. Chem. , vol.267 , pp. 9236-9240
    • Trombetta, S.E.1    Parodi, A.J.2
  • 37
    • 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., and Williams, D.B. (1996). The molecular chaperone calnexin facilitates folding and assembly of class I histocompatibility molecules. EMBO J. 15, 1495-1506.
    • (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
  • 38
    • 0017715437 scopus 로고
    • Influence of the heterosaccharides in porcine pancreatic ribonuclease on the conformation and stability of the protein
    • Wang, F.F.C., and Hirs, C.H.W. (1977). Influence of the heterosaccharides in porcine pancreatic ribonuclease on the conformation and stability of the protein. J. Biol. Chem. 252, 8358-8364.
    • (1977) J. Biol. Chem. , vol.252 , pp. 8358-8364
    • Wang, F.F.C.1    Hirs, C.H.W.2
  • 40
    • 0028278179 scopus 로고
    • Molecular cloning of a novel Ca(2+)-binding protein (calmegin) specifically expressed during male meiotic germ cell development
    • Watanabe, D., Yamada, K., Nishina, Y., Tajima, Y., Koshimizu, U., Nagata, A., and Nishimune, Y. (1994). Molecular cloning of a novel Ca(2+)-binding protein (calmegin) specifically expressed during male meiotic germ cell development. J. Biol. Chem. 269, 7744-7749.
    • (1994) J. Biol. Chem. , vol.269 , pp. 7744-7749
    • Watanabe, D.1    Yamada, K.2    Nishina, Y.3    Tajima, Y.4    Koshimizu, U.5    Nagata, A.6    Nishimune, Y.7
  • 41
    • 0023665255 scopus 로고
    • The crystal structure of ribonuclease B at 2.5-Å resolution
    • Williams, R.L, Greene, S.M., and McPherson, A. (1987). The crystal structure of ribonuclease B at 2.5-Å resolution. J. Biol. Chem. 262, 16020-16031.
    • (1987) J. Biol. Chem. , vol.262 , pp. 16020-16031
    • Williams, R.L.1    Greene, S.M.2    McPherson, A.3
  • 42
    • 0024327716 scopus 로고
    • Bromoconduritol treatment delays intracellular transport of secretory glycoproteins in human hepatoma cell cultures
    • Yeo, K.T., Yeo, T.K., and Olden, K. (1989). Bromoconduritol treatment delays intracellular transport of secretory glycoproteins in human hepatoma cell cultures. Biochem. Biophys. Res. Comm. 161, 1013-1019.
    • (1989) Biochem. Biophys. Res. Comm. , vol.161 , pp. 1013-1019
    • Yeo, K.T.1    Yeo, T.K.2    Olden, K.3
  • 43
    • 0028906481 scopus 로고
    • Calnexin recognizes carbohydrate and protein determinants of class I major histocompatibility complex molecules
    • Zhang, Q., Tector, M., and Salter, R.D. (1995). Calnexin recognizes carbohydrate and protein determinants of class I major histocompatibility complex molecules. J. Biol. Chem. 270, 3944-3948.
    • (1995) J. Biol. Chem. , vol.270 , pp. 3944-3948
    • Zhang, Q.1    Tector, M.2    Salter, R.D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.