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Volumn 13, Issue 9, 2003, Pages 641-646

Glycosylation efficiency of Asn-Xaa-Thr sequons is independent of distance from the C-terminus in membrane dipeptidase

Author keywords

Glycosyl phosphatidylinositol anchor; Membrane dipeptidase; N glycosylation; Oligosaccharyltransferase; Prion protein

Indexed keywords

AMINO ACID; ASPARAGINE; DIPEPTIDASE; GLYPICAN; ISOLEUCINE; MEMBRANE ENZYME; PHENYLALANINE; PRION PROTEIN; THREONINE;

EID: 0141729473     PISSN: 09596658     EISSN: None     Source Type: Journal    
DOI: 10.1093/glycob/cwg080     Document Type: Article
Times cited : (19)

References (30)
  • 1
    • 0028946717 scopus 로고
    • Intracellular folding of tissue-type plasminogen activator. Effects of disulfide bond formation on N-linked glycosylation and secretion
    • Allen, S., Naim, H.Y., and Bulleid, N.J. (1995) Intracellular folding of tissue-type plasminogen activator. Effects of disulfide bond formation on N-linked glycosylation and secretion. J. Biol. Chem., 270, 4797-4804.
    • (1995) J. Biol. Chem. , vol.270 , pp. 4797-4804
    • Allen, S.1    Naim, H.Y.2    Bulleid, N.J.3
  • 2
    • 0029090114 scopus 로고
    • Structures of the glycosyl-phosphatidylinositol anchors of porcine and human membrane dipeptidase. Interspecies comparison of the glycan core structures and further structural studies on the porcine anchor
    • Brewis, I.A., Ferguson, M.A.J., Mehlert, A., Turner, A.J., and Hooper, N.M. (1995) Structures of the glycosyl-phosphatidylinositol anchors of porcine and human membrane dipeptidase. Interspecies comparison of the glycan core structures and further structural studies on the porcine anchor. J. Biol. Chem., 270, 22946-22956.
    • (1995) J. Biol. Chem. , vol.270 , pp. 22946-22956
    • Brewis, I.A.1    Ferguson, M.A.J.2    Mehlert, A.3    Turner, A.J.4    Hooper, N.M.5
  • 4
    • 0020655657 scopus 로고
    • The membrane form of variant surface glycoproteins of Trypanosoma brucei
    • Cardoso de Almeida, M.L. and Turner, M.J. (1983) The membrane form of variant surface glycoproteins of Trypanosoma brucei. Nature, 302, 349-352.
    • (1983) Nature , vol.302 , pp. 349-352
    • Cardoso de Almeida, M.L.1    Turner, M.J.2
  • 5
    • 0025367812 scopus 로고
    • Sequence differences between glycosylated and non-glycosylated Asn-X-Thr/Ser acceptor sites: Implications for protein engineering
    • Gavel, Y. and von Heijne, G. (1990) Sequence differences between glycosylated and non-glycosylated Asn-X-Thr/Ser acceptor sites: implications for protein engineering. Protein Eng., 3, 433-442.
    • (1990) Protein Eng. , vol.3 , pp. 433-442
    • Gavel, Y.1    von Heijne, G.2
  • 6
    • 0026466143 scopus 로고
    • A mammalian homolog of SEC61p and SECYp is associated with ribosomes and nascent polypeptides during translocation
    • Gorlich, D., Prehn, S., Hartmann, E., Kalies, K.U., and Rapoport, T.A. (1992) A mammalian homolog of SEC61p and SECYp is associated with ribosomes and nascent polypeptides during translocation. Cell, 71, 489-503.
    • (1992) Cell , vol.71 , pp. 489-503
    • Gorlich, D.1    Prehn, S.2    Hartmann, E.3    Kalies, K.U.4    Rapoport, T.A.5
  • 7
    • 0035937505 scopus 로고    scopus 로고
    • Intracellular functions of N-linked glycans
    • Helenius, A. and Aebi, M. (2001) Intracellular functions of N-linked glycans. Science, 291, 2364-2369.
    • (2001) Science , vol.291 , pp. 2364-2369
    • Helenius, A.1    Aebi, M.2
  • 8
    • 0037298237 scopus 로고    scopus 로고
    • Stop-transfer efficiency of marginally hydrophobic segments depends on the length of the carboxy-terminal tail
    • Hessa, T., Monne, M., and Von Heijne, G. (2003) Stop-transfer efficiency of marginally hydrophobic segments depends on the length of the carboxy-terminal tail. EMBO Rep., 4, 178-183.
    • (2003) EMBO Rep. , vol.4 , pp. 178-183
    • Hessa, T.1    Monne, M.2    Von Heijne, G.3
  • 9
    • 0025169815 scopus 로고
    • Characterization of the glycosyl-phosphatidylinositol-anchored human renal dipeptidase reveals that it is more extensively glycosylated than the pig enzyme
    • Hooper, N.M., Keen, J.N., and Turner, A.J. (1990) Characterization of the glycosyl-phosphatidylinositol-anchored human renal dipeptidase reveals that it is more extensively glycosylated than the pig enzyme. Biochem. J., 265, 429-433.
    • (1990) Biochem. J. , vol.265 , pp. 429-433
    • Hooper, N.M.1    Keen, J.N.2    Turner, A.J.3
  • 10
    • 0028944878 scopus 로고
    • Conformational implications of asparagine-linked glycosylation
    • Imperiali, B. and Rickert, K.W. (1995) Conformational implications of asparagine-linked glycosylation. Proc. Natl Acad. Sci. USA, 92, 97-101.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 97-101
    • Imperiali, B.1    Rickert, K.W.2
  • 11
    • 0035662673 scopus 로고    scopus 로고
    • The molecular pathology of CJD: Old and new variants
    • Jackson, G.S. and Collinge, J. (2001) The molecular pathology of CJD: old and new variants. Mol. Pathol., 54, 393-399.
    • (2001) Mol. Pathol. , vol.54 , pp. 393-399
    • Jackson, G.S.1    Collinge, J.2
  • 12
    • 0023663543 scopus 로고
    • Oligosaccharyl transferase: The central enzyme in the pathway of glycoprotein assembly
    • Kaplan, H.A., Welply, J.K., and Lennarz, W.J. (1987) Oligosaccharyl transferase: the central enzyme in the pathway of glycoprotein assembly. Biochim. Biophys. Acta, 906, 161-173.
    • (1987) Biochim. Biophys. Acta , vol.906 , pp. 161-173
    • Kaplan, H.A.1    Welply, J.K.2    Lennarz, W.J.3
  • 13
    • 0032483365 scopus 로고    scopus 로고
    • Post-translational N-glycosylation of a truncated form of a peptide processing enzyme
    • Kolhekar, A.S., Quon, A.S., Berard, C.A., Mains, R.E., and Eipper, B.A. (1998) Post-translational N-glycosylation of a truncated form of a peptide processing enzyme. J. Biol. Chem., 273, 23012-23018.
    • (1998) J. Biol. Chem. , vol.273 , pp. 23012-23018
    • Kolhekar, A.S.1    Quon, A.S.2    Berard, C.A.3    Mains, R.E.4    Eipper, B.A.5
  • 14
    • 0024586221 scopus 로고
    • Ectoenzymes of the kidney microvillar membrane. Affinity purification, characterization and localization of the phospholipase C-solubilized form of renal dipeptidase
    • Littlewood, G.M., Hooper, N.M., and Turner, A.J. (1989) Ectoenzymes of the kidney microvillar membrane. Affinity purification, characterization and localization of the phospholipase C-solubilized form of renal dipeptidase. Biochem. J., 257, 361-367.
    • (1989) Biochem. J. , vol.257 , pp. 361-367
    • Littlewood, G.M.1    Hooper, N.M.2    Turner, A.J.3
  • 15
    • 0002898158 scopus 로고
    • Phospholipases that degrade the glycosyl-phosphatidylinositol anchor of membrane proteins
    • Hooper, N.M. and Turner, A.J. (Eds), IRL Press, Oxford
    • Low, M.G. (1992) Phospholipases that degrade the glycosyl-phosphatidylinositol anchor of membrane proteins. In Hooper, N.M. and Turner, A.J. (Eds), Lipid modification ofproteins: a practical approach. IRL Press, Oxford, pp. 117-154.
    • (1992) Lipid Modification of Proteins: A Practical Approach , pp. 117-154
    • Low, M.G.1
  • 16
    • 0028955427 scopus 로고
    • The 70 carboxyl-terminal amino acids of nascent secretory proteins are protected from proteolysis by the ribosome and the protein translocation apparatus of the endoplasmic reticulum membrane
    • Matlack, K.E. and Walter, P. (1995) The 70 carboxyl-terminal amino acids of nascent secretory proteins are protected from proteolysis by the ribosome and the protein translocation apparatus of the endoplasmic reticulum membrane. J. Biol. Chem., 270, 6170-6180.
    • (1995) J. Biol. Chem. , vol.270 , pp. 6170-6180
    • Matlack, K.E.1    Walter, P.2
  • 17
    • 0034625413 scopus 로고    scopus 로고
    • Glycosylation efficiency of Asn-Xaa-Thr sequons depends both on the distance from the C terminus and on the presence of a downstream transmembrane segment
    • Nilsson, I. and von Heijne, G. (2000) Glycosylation efficiency of Asn-Xaa-Thr sequons depends both on the distance from the C terminus and on the presence of a downstream transmembrane segment. J. Biol. Chem., 275, 17338-17343.
    • (2000) J. Biol. Chem. , vol.275 , pp. 17338-17343
    • Nilsson, I.1    von Heijne, G.2
  • 18
    • 0036382767 scopus 로고    scopus 로고
    • Crystal structure of human renal dipeptidase involved in beta-lactam hydrolysis
    • Nitanai, Y., Satow, Y., Adachi, H., and Tsujimoto, M. (2002) Crystal structure of human renal dipeptidase involved in beta-lactam hydrolysis. J. Mol. Biol., 321, 177-184.
    • (2002) J. Mol. Biol. , vol.321 , pp. 177-184
    • Nitanai, Y.1    Satow, Y.2    Adachi, H.3    Tsujimoto, M.4
  • 19
    • 0038182535 scopus 로고    scopus 로고
    • Conformation-dependent post-translational Glycosylation of tyrosinase. Requirement of a specific interaction involving the CuB metal binding site
    • Olivares, C., Solano, F., and Garcia-Borron, J.C. (2003) Conformation-dependent post-translational Glycosylation of tyrosinase. Requirement of a specific interaction involving the CuB metal binding site. J. Biol. Chem., 278, 15735-15743.
    • (2003) J. Biol. Chem. , vol.278 , pp. 15735-15743
    • Olivares, C.1    Solano, F.2    Garcia-Borron, J.C.3
  • 20
    • 0035881463 scopus 로고    scopus 로고
    • Roles of the juxtamembrane and extracellular domains of angiotensin-converting enzyme in ectodomain shedding
    • Pang, S., Chubb, A.J., Schwager, S.L.U., Ehlers, M.R.W., Sturrock, E.D., and Hooper, N.M. (2001) Roles of the juxtamembrane and extracellular domains of angiotensin-converting enzyme in ectodomain shedding. Biochem. J., 358, 185-192.
    • (2001) Biochem. J. , vol.358 , pp. 185-192
    • Pang, S.1    Chubb, A.J.2    Schwager, S.L.U.3    Ehlers, M.R.W.4    Sturrock, E.D.5    Hooper, N.M.6
  • 22
    • 0025109573 scopus 로고
    • cDNA cloning and expression in Xenopus laevis oocytes of pig renal dipeptidase, a glycosyl-phosphatidylinositol-anchored ectoenzyme
    • Rached, E., Hooper, N.M., James, P., Semenza, G., Turner, A.J., and Mantei, N. (1990) cDNA cloning and expression in Xenopus laevis oocytes of pig renal dipeptidase, a glycosyl-phosphatidylinositol-anchored ectoenzyme. Biochem. J., 271, 755-760.
    • (1990) Biochem. J. , vol.271 , pp. 755-760
    • Rached, E.1    Hooper, N.M.2    James, P.3    Semenza, G.4    Turner, A.J.5    Mantei, N.6
  • 23
    • 0030027934 scopus 로고    scopus 로고
    • Bicistronic vector for the creation of stable mammalian cell lines that predisposes all antibiotic-resistant cells to express recombinant protein
    • Rees, S., Coote, J., Stables, J., Goodson, S., Harris, S., and Lee, M.G. (1996) Bicistronic vector for the creation of stable mammalian cell lines that predisposes all antibiotic-resistant cells to express recombinant protein. Biotechniques, 20, 102-104.
    • (1996) Biotechniques , vol.20 , pp. 102-104
    • Rees, S.1    Coote, J.2    Stables, J.3    Goodson, S.4    Harris, S.5    Lee, M.G.6
  • 25
    • 0029916898 scopus 로고    scopus 로고
    • The amino acid at the X position of an Asn-X-Ser sequon is an important determinant of N-linked core-glycosylation efficiency
    • Shakin-Eshleman, S.H., Spitalnik, S.L., and Kasturi, L. (1996) The amino acid at the X position of an Asn-X-Ser sequon is an important determinant of N-linked core-glycosylation efficiency. J. Biol. Chem., 271, 6363-6366.
    • (1996) J. Biol. Chem. , vol.271 , pp. 6363-6366
    • Shakin-Eshleman, S.H.1    Spitalnik, S.L.2    Kasturi, L.3
  • 26
    • 0029991763 scopus 로고    scopus 로고
    • Biochemistry, molecular biology, and genetics of the oligosaccharyltransferase
    • Silberstein, S. and Gilmore, R. (1996) Biochemistry, molecular biology, and genetics of the oligosaccharyltransferase. FASEB J., 10, 849-858.
    • (1996) FASEB J. , vol.10 , pp. 849-858
    • Silberstein, S.1    Gilmore, R.2
  • 27
    • 0023663071 scopus 로고
    • Scrapie prion protein contains a phosphatidylinositol glycolipid
    • Stahl, N., Borchelt, D.R., Hsiao, K., and Prusiner, S.B. (1987) Scrapie prion protein contains a phosphatidylinositol glycolipid. Cell, 51, 229-240.
    • (1987) Cell , vol.51 , pp. 229-240
    • Stahl, N.1    Borchelt, D.R.2    Hsiao, K.3    Prusiner, S.B.4
  • 28
    • 0037442534 scopus 로고    scopus 로고
    • Distance of sequons to the C-terminus influences the cellular N-glycosylation of the prion protein
    • Walmsley, A.R. and Hooper, N.M. (2003) Distance of sequons to the C-terminus influences the cellular N-glycosylation of the prion protein. Biochem. J., 370, 351-355.
    • (2003) Biochem. J. , vol.370 , pp. 351-355
    • Walmsley, A.R.1    Hooper, N.M.2
  • 29
    • 0035865271 scopus 로고    scopus 로고
    • Membrane topology influences N-glycosylation of the prion protein
    • Walmsley, A.R., Zeng, F., and Hooper, N.M. (2001) Membrane topology influences N-glycosylation of the prion protein. EMBO J., 20, 703-712.
    • (2001) EMBO J. , vol.20 , pp. 703-712
    • Walmsley, A.R.1    Zeng, F.2    Hooper, N.M.3
  • 30
    • 0029983258 scopus 로고    scopus 로고
    • A nascent secretory protein may traverse the ribosome/endoplasmic reticulum translocase complex as an extended chain
    • whitley, P., Nilsson, I.M., and von Heijne, G. (1996) A nascent secretory protein may traverse the ribosome/endoplasmic reticulum translocase complex as an extended chain. J. Biol. Chem., 271, 6241-6244.
    • (1996) J. Biol. Chem. , vol.271 , pp. 6241-6244
    • whitley, P.1    Nilsson, I.M.2    von Heijne, G.3


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