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Volumn 10, Issue 5, 2000, Pages 531-538

Minimal structural and glycosylation requirements for ST6Gal I activity and trafficking

Author keywords

Activity; Glycosylation; ST6Gal; Transport

Indexed keywords

AMINO ACID; GLYCOSYLATED PROTEIN; MUTANT PROTEIN; OLIGOSACCHARIDE; SIALYLTRANSFERASE;

EID: 0034007030     PISSN: 09596658     EISSN: None     Source Type: Journal    
DOI: 10.1093/glycob/10.5.531     Document Type: Article
Times cited : (40)

References (29)
  • 1
    • 0033606823 scopus 로고    scopus 로고
    • N-glycans mediate the apical sorting of a GPI-anchored, raft-associated protein in Madin-Darby canine kidney cells
    • Benting, J.H., Rietveld, A.G. and Simons, K. (1999) N-glycans mediate the apical sorting of a GPI-anchored, raft-associated protein in Madin-Darby canine kidney cells. J. Cell Biol., 146, 313-320.
    • (1999) J. Cell Biol. , vol.146 , pp. 313-320
    • Benting, J.H.1    Rietveld, A.G.2    Simons, K.3
  • 2
    • 0034607646 scopus 로고    scopus 로고
    • Formation of insoluble oligomers correlates with ST6GalI stable localization in the Golgi
    • forthcoming
    • Chen, C., Ma, J., Lazic, A., Backovic, M. and Colley, K.J. (2000) Formation of insoluble oligomers correlates with ST6GalI stable localization in the Golgi. J. Biol. Chem., forthcoming.
    • (2000) J. Biol. Chem.
    • Chen, C.1    Ma, J.2    Lazic, A.3    Backovic, M.4    Colley, K.J.5
  • 4
    • 0026738935 scopus 로고
    • The signal anchor and stem regions of the β-galactoside α-2, 6-sialyltransferase may each act to localize the enzyme to the Golgi apparatus
    • Colley, K.J., Lee, E.U. and Paulson, J.C. (1992) The signal anchor and stem regions of the β-galactoside α-2, 6-sialyltransferase may each act to localize the enzyme to the Golgi apparatus. J. Biol. Chem., 267, 7784-7793.
    • (1992) J. Biol. Chem. , vol.267 , pp. 7784-7793
    • Colley, K.J.1    Lee, E.U.2    Paulson, J.C.3
  • 5
    • 0027370882 scopus 로고
    • Specific sequences in the signal anchor of the β-galactoside α-2,6-sialyltransferase are not essential for Golgi localization
    • Dahdal, R.Y. and Colley, K.J. (1993) Specific sequences in the signal anchor of the β-galactoside α-2,6-sialyltransferase are not essential for Golgi localization. J. Biol. Chem., 268, 26310-26319.
    • (1993) J. Biol. Chem. , vol.268 , pp. 26310-26319
    • Dahdal, R.Y.1    Colley, K.J.2
  • 6
    • 0027449104 scopus 로고
    • The role of the carbohydrate chains of Galβ-1,4-GlcNAcα2,6-sialyltransferase for enzyme activity
    • Fast, D.G., Jamieson, J.C. and McCaffrey, G. (1993) The role of the carbohydrate chains of Galβ-1,4-GlcNAcα2,6-sialyltransferase for enzyme activity. Biochim. Biophys. Acta, 1202, 325-330.
    • (1993) Biochim. Biophys. Acta , vol.1202 , pp. 325-330
    • Fast, D.G.1    Jamieson, J.C.2    McCaffrey, G.3
  • 7
    • 0029053448 scopus 로고
    • The role of N-glycans in the secretory pathway
    • Fiedler, K. and Simons, K. (1995) The role of N-glycans in the secretory pathway. Cell. 81, 309-312.
    • (1995) Cell. , vol.81 , pp. 309-312
    • Fiedler, K.1    Simons, K.2
  • 8
    • 0033168184 scopus 로고    scopus 로고
    • Crystal structures of the bovine β4galactosyltransferase catalytic domain and its complex with uridine diphosphogalactose
    • Gastinel, L.N., Cambillau, C. and Bourne, Y. (1999) Crystal structures of the bovine β4galactosyltransferase catalytic domain and its complex with uridine diphosphogalactose. EMBO J., 18, 3546-3557.
    • (1999) EMBO J. , vol.18 , pp. 3546-3557
    • Gastinel, L.N.1    Cambillau, C.2    Bourne, Y.3
  • 9
    • 0021742462 scopus 로고
    • Conversion of a secretory protein into a transmembrane protein results in its transport to the Golgi complex but not to the cell surface
    • Guan, J.-L. and Rose, J.K. (1984) Conversion of a secretory protein into a transmembrane protein results in its transport to the Golgi complex but not to the cell surface. Cell, 37, 779-787.
    • (1984) Cell , vol.37 , pp. 779-787
    • Guan, J.-L.1    Rose, J.K.2
  • 10
    • 0022130861 scopus 로고
    • Glycosylation allows cell-surface transport of an anchored secretory protein
    • Guan, J.-L., Machamer, C.E. and Rose, J.K. (1985) Glycosylation allows cell-surface transport of an anchored secretory protein. Cell, 42, 489-496.
    • (1985) Cell , vol.42 , pp. 489-496
    • Guan, J.-L.1    Machamer, C.E.2    Rose, J.K.3
  • 11
    • 0032055472 scopus 로고    scopus 로고
    • Carbohydrate-mediated Golgi to cell surface transport and apical targeting of membrane proteins
    • Gut, A., Kappeler, F., Hyka, N., Balda, M.S., Hauri, H.-P. and Matter, K. (1998) Carbohydrate-mediated Golgi to cell surface transport and apical targeting of membrane proteins. EMBO J., 17, 1919-1929.
    • (1998) EMBO J. , vol.17 , pp. 1919-1929
    • Gut, A.1    Kappeler, F.2    Hyka, N.3    Balda, M.S.4    Hauri, H.-P.5    Matter, K.6
  • 12
    • 0028880799 scopus 로고
    • The effects of the site-directed removal of N-glycosylation sites from β-1,4-N-acetylgalactosminyltransferase on its function
    • Haraguchi, M., Yamashiro, S., Furukawa, K., Takamiya, K., Shiku, H. and Furukawa, K. (1995) The effects of the site-directed removal of N-glycosylation sites from β-1,4-N-acetylgalactosminyltransferase on its function. Biochem. J., 312, 273-280.
    • (1995) Biochem. J. , vol.312 , pp. 273-280
    • Haraguchi, M.1    Yamashiro, S.2    Furukawa, K.3    Takamiya, K.4    Shiku, H.5    Furukawa, K.6
  • 14
    • 0021891884 scopus 로고
    • Assembly of asparagine-linked oligosaccharides
    • Kornfeld, S. and Kornfeld, R. (1985) Assembly of asparagine-linked oligosaccharides. Annu. Rev. Biochem., 54, 631-664.
    • (1985) Annu. Rev. Biochem. , vol.54 , pp. 631-664
    • Kornfeld, S.1    Kornfeld, R.2
  • 15
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 16
    • 0024321508 scopus 로고
    • Alteration of terminal glycosylation sequences on N-linked oligosaccharides of Chinese hamster ovary cells by expression of β-galactoside α2,6-sialyltransferase
    • Lee, E.U., Roth, J. and Paulson, J.C. (1989) Alteration of terminal glycosylation sequences on N-linked oligosaccharides of Chinese hamster ovary cells by expression of β-galactoside α2,6-sialyltransferase. J. Biol. Chem., 264, 13848-13855.
    • (1989) J. Biol. Chem. , vol.264 , pp. 13848-13855
    • Lee, E.U.1    Roth, J.2    Paulson, J.C.3
  • 17
    • 0029871352 scopus 로고    scopus 로고
    • A disulfide-bonded dimer of the Golgi β-galactoside α2, 6-sialyltransferase is catalytically inactive yet still retains the ability to bind galactose
    • Ma, J. and Colley, K.J. (1996) A disulfide-bonded dimer of the Golgi β-galactoside α2, 6-sialyltransferase is catalytically inactive yet still retains the ability to bind galactose. J. Biol. Chem., 271, 7758-7766.
    • (1996) J. Biol. Chem. , vol.271 , pp. 7758-7766
    • Ma, J.1    Colley, K.J.2
  • 18
    • 0030614460 scopus 로고    scopus 로고
    • Two naturally occurring α2, 6-sialyltransferase forms with a single amino acid change in the catalytic domain differ in their catalytic activity and proteolytic processing
    • Ma, J., Qian, R., Rausa, F.M. and Colley, K.J. (1997) Two naturally occurring α2, 6-sialyltransferase forms with a single amino acid change in the catalytic domain differ in their catalytic activity and proteolytic processing. J. Biol. Chem., 272, 672-679.
    • (1997) J. Biol. Chem. , vol.272 , pp. 672-679
    • Ma, J.1    Qian, R.2    Rausa, F.M.3    Colley, K.J.4
  • 19
    • 0024336222 scopus 로고
    • Characterization of glycoproteins and their associated oligosaccharides through the use of endoglycosidases
    • Maley, F., Trimble, R.B., Tarentino, A.L. and Plummer, T.H., Jr. (1989) Characterization of glycoproteins and their associated oligosaccharides through the use of endoglycosidases. Anal. Biochem., 180, 195-204.
    • (1989) Anal. Biochem. , vol.180 , pp. 195-204
    • Maley, F.1    Trimble, R.B.2    Tarentino, A.L.3    Plummer T.H., Jr.4
  • 20
    • 0032488983 scopus 로고    scopus 로고
    • Influence of N-glycosylation and N-glycan trimming on the activity and intracellular traffic of GD3 synthase
    • Martina, J.A., Daniotti, J.L. and Maccioni, H.J.F. (1998) Influence of N-glycosylation and N-glycan trimming on the activity and intracellular traffic of GD3 synthase. J. Biol. Chem., 273, 3725-3731.
    • (1998) J. Biol. Chem. , vol.273 , pp. 3725-3731
    • Martina, J.A.1    Daniotti, J.L.2    Maccioni, H.J.F.3
  • 21
    • 0027172770 scopus 로고
    • Mutational analysts of the Golgi retention signal of bovine β1,4-galactosyltransferase
    • Masibay, A.S., Balaji, P.J., Boeggeman, E.E. and Quasba, P.K. (1993) Mutational analysts of the Golgi retention signal of bovine β1,4-galactosyltransferase. J. Biol. Chem., 268, 9908-9916.
    • (1993) J. Biol. Chem. , vol.268 , pp. 9908-9916
    • Masibay, A.S.1    Balaji, P.J.2    Boeggeman, E.E.3    Quasba, P.K.4
  • 22
    • 0030884364 scopus 로고    scopus 로고
    • N-Glycosylation is requisite for the enzyme activity and Golgi retention of N-acetylglucosyaminyltransferase III
    • Nagai, K., Ihara, Y., Wada, Y. and Taniguchi, N. (1997) N-Glycosylation is requisite for the enzyme activity and Golgi retention of N-acetylglucosyaminyltransferase III. Glycobiology, 7, 769-776.
    • (1997) Glycobiology , vol.7 , pp. 769-776
    • Nagai, K.1    Ihara, Y.2    Wada, Y.3    Taniguchi, N.4
  • 23
    • 0033179221 scopus 로고    scopus 로고
    • Glycans in post-Golgi apical targeting: Sorting signals or structural props?
    • Rodriguez-Boulan, E. and Gonzalez, A. (1999) Glycans in post-Golgi apical targeting: sorting signals or structural props? Trends Cell Biol., 9, 291-294.
    • (1999) Trends Cell Biol. , vol.9 , pp. 291-294
    • Rodriguez-Boulan, E.1    Gonzalez, A.2
  • 24
    • 0028810337 scopus 로고
    • N-glycans as apical sorting signals in epithelial cells
    • Scheiffele, P., Peranen, J. and Simons, K. (1995) N-glycans as apical sorting signals in epithelial cells. Nature, 378, 96-98.
    • (1995) Nature , vol.378 , pp. 96-98
    • Scheiffele, P.1    Peranen, J.2    Simons, K.3
  • 26
    • 0030752110 scopus 로고    scopus 로고
    • Expression of stable human O-glycan core 2 β-1.6-N-acetylglucosaminyltransferase in Sf9 insect cells
    • Toki, D., Sarkar, M., Yip, B., Reck, F. Joziasse, D., Fukuda, M., Schachter, H. and Brockhausen, I. (1997) Expression of stable human O-glycan core 2 β-1.6-N-acetylglucosaminyltransferase in Sf9 insect cells. Biochem. J., 325, 63-69.
    • (1997) Biochem. J. , vol.325 , pp. 63-69
    • Toki, D.1    Sarkar, M.2    Yip, B.3    Reck, F.4    Joziasse, D.5    Fukuda, M.6    Schachter, H.7    Brockhausen, I.8
  • 27
    • 0027318961 scopus 로고
    • Biological roles of oligosaccharides: All theories are correct
    • Varki, A. (1993) Biological roles of oligosaccharides: all theories are correct. Glycobiology, 3, 97-130.
    • (1993) Glycobiology , vol.3 , pp. 97-130
    • Varki, A.1
  • 28
  • 29
    • 0030726211 scopus 로고    scopus 로고
    • The O-glycosylated stalk domain is required for apical sorting of neurotropin receptors in polarized MDCK cells
    • Yeaman, C., Le Gall, A.H., Baldwin, A.N., Monlauzeur, L., Le Bivic, A. and Rodriguez-Boulan, E. (1997) The O-glycosylated stalk domain is required for apical sorting of neurotropin receptors in polarized MDCK cells. J. Cell Biol., 139, 929-940.
    • (1997) J. Cell Biol. , vol.139 , pp. 929-940
    • Yeaman, C.1    Le Gall, A.H.2    Baldwin, A.N.3    Monlauzeur, L.4    Le Bivic, A.5    Rodriguez-Boulan, E.6


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