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Volumn 147, Issue 3, 2010, Pages 337-344

Role of N-glycans in maintaining the activity of protein O-mannosyltransferases POMT1 and POMT2

Author keywords

N glycosylation; POMT1; POMT2; Protein O mannosyltransferase; Secondary structure

Indexed keywords

GLYCAN; GLYCAN DERIVATIVE; MANNOSYLTRANSFERASE; PROTEIN O MANNOSYLTRANSFERASE 1; PROTEIN O MANNOSYLTRANSFERASE 2; UNCLASSIFIED DRUG;

EID: 77249095040     PISSN: 0021924X     EISSN: 17562651     Source Type: Journal    
DOI: 10.1093/jb/mvp170     Document Type: Article
Times cited : (18)

References (28)
  • 1
    • 0347635516 scopus 로고    scopus 로고
    • Demonstration of mammalian protein O-mannosyltransferase activity: Coexpression of POMT1 and POMT2 required for enzymatic activity
    • Manya, H., Chiba, A., Yoshida, A., Wang, X., Chiba, Y., Jigami, Y., Margolis, R.U., and Endo, T. (2004) Demonstration of mammalian protein O-mannosyltransferase activity: coexpression of POMT1 and POMT2 required for enzymatic activity. Proc. Natl Acad. Sci. USA 101, 500-505
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 500-505
    • Manya, H.1    Chiba, A.2    Yoshida, A.3    Wang, X.4    Chiba, Y.5    Jigami, Y.6    Margolis, R.U.7    Endo, T.8
  • 4
    • 0031026624 scopus 로고    scopus 로고
    • Structures of sialylated O-linked oligosaccharides of bovine peripheral nerve a-dystroglycan. The role of a novel O-mannosyl-type oligosaccharide in the binding of a-dystroglycan with laminin
    • Chiba, A., Matsumura, K., Yamada, H., Inazu, T., Shimizu, T., Kusunoki, S., Kanazawa, I., Kobata, A., and Endo, T. (1997) Structures of sialylated O-linked oligosaccharides of bovine peripheral nerve a-dystroglycan. The role of a novel O-mannosyl-type oligosaccharide in the binding of a-dystroglycan with laminin. J. Biol. Chem. 272, 2156-2162
    • (1997) J. Biol. Chem. , vol.272 , pp. 2156-2162
    • Chiba, A.1    Matsumura, K.2    Yamada, H.3    Inazu, T.4    Shimizu, T.5    Kusunoki, S.6    Kanazawa, I.7    Kobata, A.8    Endo, T.9
  • 5
    • 5444247077 scopus 로고    scopus 로고
    • Structure, function and pathology of O-mannosyl glycans
    • Endo, T. (2004) Structure, function and pathology of O-mannosyl glycans. Glycoconj. J. 21, 3-7
    • (2004) Glycoconj. J. , vol.21 , pp. 3-7
    • Endo, T.1
  • 7
    • 0038182574 scopus 로고    scopus 로고
    • Dystrophin-glycoprotein complex: Post-translational processing and dystroglycan function
    • Michele, D.E. and Campbell, K.P. (2003) Dystrophin-glycoprotein complex: post-translational processing and dystroglycan function. J. Biol. Chem. 278, 15457-15460
    • (2003) J. Biol. Chem. , vol.278 , pp. 15457-15460
    • Michele, D.E.1    Campbell, K.P.2
  • 8
    • 0029063024 scopus 로고
    • Electron microscopic evidence for a mucin-like region in chick muscle a-dystroglycan
    • Brancaccio, A., Schulthess, T., Gesemann, M., and Engel, J. (1995) Electron microscopic evidence for a mucin-like region in chick muscle a-dystroglycan. FEBS Lett. 368, 139-142
    • (1995) FEBS Lett. , vol.368 , pp. 139-142
    • Brancaccio, A.1    Schulthess, T.2    Gesemann, M.3    Engel, J.4
  • 9
    • 0030916837 scopus 로고    scopus 로고
    • The N-terminal region of a-dystroglycan is an autonomous globular domain
    • Brancaccio, A., Schulthess, T., Gesemann, M., and Engel, J. (1997) The N-terminal region of a-dystroglycan is an autonomous globular domain. Eur. J. Biochem. 246, 166-172
    • (1997) Eur. J. Biochem. , vol.246 , pp. 166-172
    • Brancaccio, A.1    Schulthess, T.2    Gesemann, M.3    Engel, J.4
  • 12
    • 33344477191 scopus 로고    scopus 로고
    • Aberrant glycosylation of a-dystroglycan and congenital muscular dystrophies
    • Endo, T. (2005) Aberrant glycosylation of a-dystroglycan and congenital muscular dystrophies. Acta. Myol. 24, 64-69
    • (2005) Acta. Myol. , vol.24 , pp. 64-69
    • Endo, T.1
  • 14
    • 7444229243 scopus 로고    scopus 로고
    • Mutations of the POMT1 gene found in patients with Walker-Warburg syndrome lead to a defect of protein O-mannosylation
    • Akasaka-Manya, K., Manya, H., and Endo, T. (2004) Mutations of the POMT1 gene found in patients with Walker-Warburg syndrome lead to a defect of protein O-mannosylation. Biochem. Biophys. Res. Commun. 325, 75-79
    • (2004) Biochem. Biophys. Res. Commun. , vol.325 , pp. 75-79
    • Akasaka-Manya, K.1    Manya, H.2    Endo, T.3
  • 15
    • 33745817404 scopus 로고    scopus 로고
    • Physical and functional association of human protein O- mannosyltransferases 1 and 2
    • Akasaka-Manya, K., Manya, H., Nakajima, A., Kawakita, M., and Endo, T. (2006) Physical and functional association of human protein O- mannosyltransferases 1 and 2. J. Biol. Chem. 281, 19339-19345
    • (2006) J. Biol. Chem. , vol.281 , pp. 19339-19345
    • Akasaka-Manya, K.1    Manya, H.2    Nakajima, A.3    Kawakita, M.4    Endo, T.5
  • 17
    • 0033605720 scopus 로고    scopus 로고
    • Transmembrane topology of pmt1p, a member of an evolutionarily conserved family of protein O-mannosyltransferases
    • Strahl-Bolsinger, S. and Scheinost, A. (1999) Transmembrane topology of pmt1p, a member of an evolutionarily conserved family of protein O-mannosyltransferases. J. Biol. Chem. 274, 9068-9075
    • (1999) J. Biol. Chem. , vol.274 , pp. 9068-9075
    • Strahl-Bolsinger, S.1    Scheinost, A.2
  • 18
    • 0038823596 scopus 로고    scopus 로고
    • Members of the evolutionarily conserved PMT family of protein O-Mannosyltransferases form distinct protein complexes among themselves
    • Girrbach, V. and Strahl, S. (2003) Members of the evolutionarily conserved PMT family of protein O-Mannosyltransferases form distinct protein complexes among themselves. J. Biol. Chem. 278, 12554-12562
    • (2003) J. Biol. Chem. , vol.278 , pp. 12554-12562
    • Girrbach, V.1    Strahl, S.2
  • 19
    • 0034705478 scopus 로고    scopus 로고
    • Structure-function analysis of the dolichyl phosphate-mannose: Protein O-mannosyltransferase ScPmt1p
    • Girrbach, V., Zeller, T., Priesmeier, M., and Strahl-Bolsinger, S. (2000) Structure-function analysis of the dolichyl phosphate-mannose: protein O-mannosyltransferase ScPmt1p. J. Biol. Chem. 275, 19288-19296
    • (2000) J. Biol. Chem. , vol.275 , pp. 19288-19296
    • Girrbach, V.1    Zeller, T.2    Priesmeier, M.3    Strahl-Bolsinger, S.4
  • 20
    • 0031826040 scopus 로고    scopus 로고
    • SOSUI: Classification and secondary structure prediction system for membrane proteins
    • Hirokawa, T., Boon-Chieng, S., and Mitaku, S. (1998) SOSUI: classification and secondary structure prediction system for membrane proteins. Bioinformatics 14, 378-379
    • (1998) Bioinformatics , vol.14 , pp. 378-379
    • Hirokawa, T.1    Boon-Chieng, S.2    Mitaku, S.3
  • 21
    • 0000207681 scopus 로고
    • TMbase - A database of membrane spanning proteins segments
    • Hofmann, K. and Stoffel, W. (1993) TMbase - a database of membrane spanning proteins segments. Biol. Chem. Hoppe-Seyler 374, 166
    • (1993) Biol. Chem. Hoppe-Seyler , vol.374 , pp. 166
    • Hofmann, K.1    Stoffel, W.2
  • 22
    • 0034786532 scopus 로고    scopus 로고
    • The HMMTOP transmembrane topology prediction server
    • Tusnady, G.E. and Simon, I. (2001) The HMMTOP transmembrane topology prediction server. Bioinformatics 17, 849-850
    • (2001) Bioinformatics , vol.17 , pp. 849-850
    • Tusnady, G.E.1    Simon, I.2
  • 23
    • 0027417476 scopus 로고
    • Determination of the distance between the oligosaccharyltransferase active site and the endoplasmic reticulum membrane
    • Nilsson, I.M. and von Heijne, G. (1993) Determination of the distance between the oligosaccharyltransferase active site and the endoplasmic reticulum membrane. J. Biol. Chem. 268, 5798-5801
    • (1993) J. Biol. Chem. , vol.268 , pp. 5798-5801
    • Nilsson, I.M.1    Von Heijne, G.2
  • 24
    • 0018632963 scopus 로고
    • Use of endo- and exoglycosidases for structural studies of glycoconjugates
    • Kobata, A. (1979) Use of endo- and exoglycosidases for structural studies of glycoconjugates. Anal. Biochem. 100, 1-14
    • (1979) Anal. Biochem. , vol.100 , pp. 1-14
    • Kobata, A.1
  • 25
    • 0021485787 scopus 로고
    • Optimizing hydrolysis of N-linked high-mannose oligosaccharides by endo-b-N-acetylglucosaminidase H
    • Trimble, R.B. and Maley, F. (1984) Optimizing hydrolysis of N-linked high-mannose oligosaccharides by endo-b-N-acetylglucosaminidase H. Anal. Biochem. 141, 515-522
    • (1984) Anal. Biochem. , vol.141 , pp. 515-522
    • Trimble, R.B.1    Maley, F.2
  • 26
    • 23244440497 scopus 로고    scopus 로고
    • Export-mediated assembly of mycobacterial glycoproteins parallels eukaryotic pathways
    • VanderVen, B.C., Harder, J.D., Crick, D.C., and Belisle, J.T. (2005) Export-mediated assembly of mycobacterial glycoproteins parallels eukaryotic pathways. Science 309, 941-943
    • (2005) Science , vol.309 , pp. 941-943
    • Vander Ven, B.C.1    Harder, J.D.2    Crick, D.C.3    Belisle, J.T.4
  • 27
    • 0025973305 scopus 로고
    • Protein O-glycosylation in Saccharomyces cerevisiae. Purification and characterization of the dolichylphosphate- D-mannose-protein O-D-mannosyltransferase
    • Strahl-Bolsinger, S. and Tanner, W. (1991) Protein O-glycosylation in Saccharomyces cerevisiae. Purification and characterization of the dolichylphosphate- D-mannose-protein O-D-mannosyltransferase. Eur. J. Biochem. 196, 185-190
    • (1991) Eur. J. Biochem. , vol.196 , pp. 185-190
    • Strahl-Bolsinger, S.1    Tanner, W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.