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Volumn 288, Issue 8, 2013, Pages 5828-5839

Proprotein convertases process and thereby inactivate formylglycine- generating enzyme

Author keywords

[No Author keywords available]

Indexed keywords

CONVERTASES; FORMYLGLYCINE-GENERATING ENZYMES; SULFATASES;

EID: 84874293596     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.405159     Document Type: Article
Times cited : (10)

References (36)
  • 1
    • 0032104543 scopus 로고    scopus 로고
    • A novel protein modification generating an aldehyde group in sulfatases: Its role in catalysis and disease
    • von Figura, K., Schmidt, B., Selmer, T., and Dierks, T. (1998) A novel protein modification generating an aldehyde group in sulfatases: Its role in catalysis and disease. BioEssays 20, 505-510
    • (1998) BioEssays , vol.20 , pp. 505-510
    • Von Figura, K.1    Schmidt, B.2    Selmer, T.3    Dierks, T.4
  • 3
    • 0029130352 scopus 로고
    • A novel amino acid modification in sulfatases that is defective in multiple sulfatase deficiency
    • Schmidt, B., Selmer, T., Ingendoh, A., and von Figura, K. (1995) A novel amino acid modification in sulfatases that is defective in multiple sulfatase deficiency. Cell 82, 271-278
    • (1995) Cell , vol.82 , pp. 271-278
    • Schmidt, B.1    Selmer, T.2    Ingendoh, A.3    Von Figura, K.4
  • 4
    • 0037847425 scopus 로고    scopus 로고
    • Multiple sulfatase deficiency is caused by mutations in the gene encoding the human C(-)-formylglycine-generating enzyme
    • Dierks, T., Schmidt, B., Borissenko, L. V., Peng, J., Preusser, A., Mariappan, M., and von Figura, K. (2003) Multiple sulfatase deficiency is caused by mutations in the gene encoding the human C(-)-formylglycine-generating enzyme. Cell 113, 435-444
    • (2003) Cell , vol.113 , pp. 435-444
    • Dierks, T.1    Schmidt, B.2    Borissenko, L.V.3    Peng, J.4    Preusser, A.5    Mariappan, M.6    Von Figura, K.7
  • 5
    • 0037509873 scopus 로고    scopus 로고
    • The multiple sulfatase deficiency gene encodes an essential and limiting factor for the activity of sulfatases
    • Cosma, M. P., Pepe, S., Annunziata, I., Newbold, R. F., Grompe, M., Parenti, G., and Ballabio, A. (2003) The multiple sulfatase deficiency gene encodes an essential and limiting factor for the activity of sulfatases. Cell 113, 445-456
    • (2003) Cell , vol.113 , pp. 445-456
    • Cosma, M.P.1    Pepe, S.2    Annunziata, I.3    Newbold, R.F.4    Grompe, M.5    Parenti, G.6    Ballabio, A.7
  • 7
    • 34848837976 scopus 로고    scopus 로고
    • Multiple sulfatase deficiency is due to hypomorphic mutations of the SUMF1 gene
    • Annunziata, I., Bouche, V., Lombardi, A., Settembre, C., and Ballabio, A. (2007) Multiple sulfatase deficiency is due to hypomorphic mutations of the SUMF1 gene. Hum. Mutat. 28, 928
    • (2007) Hum. Mutat. , vol.28 , pp. 928
    • Annunziata, I.1    Bouche, V.2    Lombardi, A.3    Settembre, C.4    Ballabio, A.5
  • 8
    • 38849095352 scopus 로고    scopus 로고
    • Molecular analysis of SUMF1 mutations: Stability and residual activity of mutant formylglycine-generating enzyme determine disease severity in multiple sulfatase deficiency
    • Schlotawa, L., Steinfeld, R., von Figura, K., Dierks, T., and Gärtner, J. (2008) Molecular analysis of SUMF1 mutations: Stability and residual activity of mutant formylglycine-generating enzyme determine disease severity in multiple sulfatase deficiency. Hum. Mutat. 29, 205
    • (2008) Hum. Mutat. , vol.29 , pp. 205
    • Schlotawa, L.1    Steinfeld, R.2    Von Figura, K.3    Dierks, T.4    Gärtner, J.5
  • 9
    • 77955372999 scopus 로고    scopus 로고
    • Sulfatase modifying factor 1-mediated fibroblast growth factor signaling primes hematopoietic multilineage development
    • Buono, M., Visigalli, I., Bergamasco, R., Biffi, A., and Cosma, M. P. (2010) Sulfatase modifying factor 1-mediated fibroblast growth factor signaling primes hematopoietic multilineage development. J. Exp. Med. 207, 1647-1660
    • (2010) J. Exp. Med. , vol.207 , pp. 1647-1660
    • Buono, M.1    Visigalli, I.2    Bergamasco, R.3    Biffi, A.4    Cosma, M.P.5
  • 10
    • 19344367884 scopus 로고    scopus 로고
    • Molecular basis for multiple sulfatase deficiency and mechanism for formylglycine generation of the human formylglycine-generating enzyme
    • Dierks, T., Dickmanns, A., Preusser-Kunze, A., Schmidt, B., Mariappan, M., von Figura, K., Ficner, R., and Rudolph, M. G. (2005) Molecular basis for multiple sulfatase deficiency and mechanism for formylglycine generation of the human formylglycine-generating enzyme. Cell 121, 541-552
    • (2005) Cell , vol.121 , pp. 541-552
    • Dierks, T.1    Dickmanns, A.2    Preusser-Kunze, A.3    Schmidt, B.4    Mariappan, M.5    Von Figura, K.6    Ficner, R.7    Rudolph, M.G.8
  • 11
    • 0141922853 scopus 로고    scopus 로고
    • The human SUMF1 gene, required for posttranslational sulfatase modification, defines a new gene family which is conserved from pro-to eukaryotes
    • Landgrebe, J., Dierks, T., Schmidt, B., and von Figura, K. (2003) The human SUMF1 gene, required for posttranslational sulfatase modification, defines a new gene family which is conserved from pro-to eukaryotes. Gene 316, 47-56
    • (2003) Gene , vol.316 , pp. 47-56
    • Landgrebe, J.1    Dierks, T.2    Schmidt, B.3    Von Figura, K.4
  • 12
    • 45549103883 scopus 로고    scopus 로고
    • The non-catalytic N-terminal extension of formylglycine-generating enzyme is required for its biological activity and retention in the endoplasmic reticulum
    • Mariappan, M., Gande, S. L., Radhakrishnan, K., Schmidt, B., Dierks, T., and von Figura, K. (2008) The non-catalytic N-terminal extension of formylglycine-generating enzyme is required for its biological activity and retention in the endoplasmic reticulum. J. Biol. Chem. 283, 11556-11564
    • (2008) J. Biol. Chem. , vol.283 , pp. 11556-11564
    • Mariappan, M.1    Gande, S.L.2    Radhakrishnan, K.3    Schmidt, B.4    Dierks, T.5    Von Figura, K.6
  • 13
    • 44449129593 scopus 로고    scopus 로고
    • ERp44 mediates a thiol-independent retention of formylglycine-generating enzyme in the endoplasmic reticulum
    • Mariappan, M., Radhakrishnan, K., Dierks, T., Schmidt, B., and von Figura, K. (2008) ERp44 mediates a thiol-independent retention of formylglycine-generating enzyme in the endoplasmic reticulum. J. Biol. Chem. 283, 6375-6383
    • (2008) J. Biol. Chem. , vol.283 , pp. 6375-6383
    • Mariappan, M.1    Radhakrishnan, K.2    Dierks, T.3    Schmidt, B.4    Von Figura, K.5
  • 17
    • 79952466610 scopus 로고    scopus 로고
    • What lies ahead for the proprotein convertases?
    • Seidah, N. G. (2011) What lies ahead for the proprotein convertases?. Ann. N.Y. Acad. Sci. 1220, 149-161
    • (2011) Ann. N.Y. Acad. Sci. , vol.1220 , pp. 149-161
    • Seidah, N.G.1
  • 18
    • 0035903230 scopus 로고    scopus 로고
    • Inhibition of proprotein convertases is associated with loss of growth and tumorigenicity of HT-29 human colon carcinoma cells: Importance of insulin-like growth factor-1 (IGF-1) receptor processing in IGF-1-mediated functions
    • Khatib, A. M., Siegfried, G., Prat, A., Luis, J., Chrétien, M., Metrakos, P., and Seidah, N. G. (2001) Inhibition of proprotein convertases is associated with loss of growth and tumorigenicity of HT-29 human colon carcinoma cells: Importance of insulin-like growth factor-1 (IGF-1) receptor processing in IGF-1-mediated functions. J. Biol. Chem. 276, 30686-30693
    • (2001) J. Biol. Chem. , vol.276 , pp. 30686-30693
    • Khatib, A.M.1    Siegfried, G.2    Prat, A.3    Luis, J.4    Chrétien, M.5    Metrakos, P.6    Seidah, N.G.7
  • 19
    • 0025008168 scopus 로고
    • Sequence logos: A new way to display consensus sequences
    • Schneider T. D., and Stephens R. M. (1990) Sequence logos: A new way to display consensus sequences. Nucleic Acids Res. 18, 6097-6100
    • (1990) Nucleic Acids Res. , vol.18 , pp. 6097-6100
    • Schneider, T.D.1    Stephens, R.M.2
  • 21
    • 0028872463 scopus 로고
    • Proteolytic activation of bacterial toxins by eukaryotic cells is performed by furin and by additional cellular proteases
    • Gordon, V. M., Klimpel, K. R., Arora, N., Henderson, M. A., and Leppla, S. H. (1995) Proteolytic activation of bacterial toxins by eukaryotic cells is performed by furin and by additional cellular proteases. Infect.Immun.63,82-87
    • (1995) Infect. Immun. , vol.63 , pp. 82-87
    • Gordon, V.M.1    Klimpel, K.R.2    Arora, N.3    Henderson, M.A.4    Leppla, S.H.5
  • 22
    • 0026776768 scopus 로고
    • In vitro mutagenesis of potential N-glycosylation sites of arylsulfatase A: Effects on glycosylation, phosphorylation, and intracellular sorting
    • Gieselmann, V., Schmidt, B., and von Figura, K. (1992) In vitro mutagenesis of potential N-glycosylation sites of arylsulfatase A: Effects on glycosylation, phosphorylation, and intracellular sorting. J. Biol. Chem. 267, 13262-13266
    • (1992) J. Biol. Chem. , vol.267 , pp. 13262-13266
    • Gieselmann, V.1    Schmidt, B.2    Von Figura, K.3
  • 24
    • 0842313260 scopus 로고    scopus 로고
    • Prediction of proprotein convertase cleavage sites
    • Duckert, P., Brunak, S., and Blom, N. (2004) Prediction of proprotein convertase cleavage sites. Protein Eng. Des. Sel. 17, 107-112
    • (2004) Protein Eng. Des. Sel. , vol.17 , pp. 107-112
    • Duckert, P.1    Brunak, S.2    Blom, N.3
  • 25
    • 84859735363 scopus 로고    scopus 로고
    • Computational prediction of furin cleavage sites by a hybrid method and understanding mechanism underlying diseases
    • Tian, S., Huajun, W., and Wu, J. (2012) Computational prediction of furin cleavage sites by a hybrid method and understanding mechanism underlying diseases. Sci. Rep. 2, 261
    • (2012) Sci. Rep. , vol.2 , pp. 261
    • Tian, S.1    Huajun, W.2    Wu, J.3
  • 26
    • 62949163223 scopus 로고    scopus 로고
    • Molecular basis of multiple sulfatase deficiency, mucolipidosis II/III and Niemann-Pick C1 disease: Lysosomal storage disorders caused by defects of non-lysosomal proteins
    • Dierks, T., Schlotawa, L., Frese, M. A., Radhakrishnan, K., von Figura, K., and Schmidt, B. (2009) Molecular basis of multiple sulfatase deficiency, mucolipidosis II/III and Niemann-Pick C1 disease: Lysosomal storage disorders caused by defects of non-lysosomal proteins. Biochim. Biophys. Acta 1793, 710-725
    • (2009) Biochim. Biophys. Acta , vol.1793 , pp. 710-725
    • Dierks, T.1    Schlotawa, L.2    Frese, M.A.3    Radhakrishnan, K.4    Von Figura, K.5    Schmidt, B.6
  • 27
    • 82255195530 scopus 로고    scopus 로고
    • The Cambrian conundrum: Early divergence and later ecological success in the early history of animals
    • Erwin, D. H., Laflamme, M., Tweedt, S. M., Sperling, E. A., Pisani, D., and Peterson, K. J. (2011) The Cambrian conundrum: Early divergence and later ecological success in the early history of animals. Science 334, 1091-1097
    • (2011) Science , vol.334 , pp. 1091-1097
    • Erwin, D.H.1    Laflamme, M.2    Tweedt, S.M.3    Sperling, E.A.4    Pisani, D.5    Peterson, K.J.6
  • 28
    • 0025916877 scopus 로고
    • Arg-X-Lys/Arg-Arg motif as a signal for precursor cleavage catalyzed by furin within the constitutive secretory pathway
    • Hosaka, M., Nagahama, M., Kim, W. S., Watanabe, T., Hatsuzawa, K., Ikemizu, J., Murakami, K., and Nakayama, K. (1991) Arg-X-Lys/Arg-Arg motif as a signal for precursor cleavage catalyzed by furin within the constitutive secretory pathway. J. Biol. Chem. 266, 12127-12130
    • (1991) J. Biol. Chem. , vol.266 , pp. 12127-12130
    • Hosaka, M.1    Nagahama, M.2    Kim, W.S.3    Watanabe, T.4    Hatsuzawa, K.5    Ikemizu, J.6    Murakami, K.7    Nakayama, K.8
  • 30
    • 0026775916 scopus 로고
    • Human furin is a calcium-dependent serine endoprotease that recognizes the sequence Arg-X-X-Arg and efficiently cleaves anthrax toxin protective antigen
    • Molloy, S. S., Bresnahan, P. A., Leppla, S. H., Klimpel, K. R., and Thomas, G. (1992) Human furin is a calcium-dependent serine endoprotease that recognizes the sequence Arg-X-X-Arg and efficiently cleaves anthrax toxin protective antigen. J. Biol. Chem. 267, 16396-16402
    • (1992) J. Biol. Chem. , vol.267 , pp. 16396-16402
    • Molloy, S.S.1    Bresnahan, P.A.2    Leppla, S.H.3    Klimpel, K.R.4    Thomas, G.5
  • 31
    • 0035868365 scopus 로고    scopus 로고
    • Shed furin: Mapping of the cleavage determinants and identification of its C terminus
    • Plaimauer, B., Mohr, G., Wernhart, W., Himmelspach, M., Dorner, F., and Schlokat, U. (2001) "Shed" furin: Mapping of the cleavage determinants and identification of its C terminus. Biochem. J. 354, 689-695
    • (2001) Biochem. J. , vol.354 , pp. 689-695
    • Plaimauer, B.1    Mohr, G.2    Wernhart, W.3    Himmelspach, M.4    Dorner, F.5    Schlokat, U.6
  • 32
    • 0035861743 scopus 로고    scopus 로고
    • Characterization of posttranslational formylglycine formation by luminal components of the endoplasmic reticulum
    • Fey, J., Balleininger, M., Borissenko, L. V., Schmidt, B., von Figura, K., and Dierks, T. (2001) Characterization of posttranslational formylglycine formation by luminal components of the endoplasmic reticulum. J. Biol. Chem. 276, 47021-47028
    • (2001) J. Biol. Chem. , vol.276 , pp. 47021-47028
    • Fey, J.1    Balleininger, M.2    Borissenko, L.V.3    Schmidt, B.4    Von Figura, K.5    Dierks, T.6
  • 33
    • 77649083093 scopus 로고    scopus 로고
    • Comparative study of the binding pockets of mammalian proprotein convertases and its implications for the design of specific small molecule inhibitors
    • Tian, S., and Jianhua, W. (2010) Comparative study of the binding pockets of mammalian proprotein convertases and its implications for the design of specific small molecule inhibitors. Int. J. Biol. Sci. 6, 89-95
    • (2010) Int. J. Biol. Sci. , vol.6 , pp. 89-95
    • Tian, S.1    Jianhua, W.2
  • 35
    • 62549121136 scopus 로고    scopus 로고
    • Site-specific chemical modification of recombinant proteins produced in mammalian cells by using the genetically encoded aldehyde tag
    • Wu, P., Shui, W., Carlson, B. L., Hu, N., Rabuka, D., Lee, J., and Bertozzi, C. R. (2009) Site-specific chemical modification of recombinant proteins produced in mammalian cells by using the genetically encoded aldehyde tag. Proc. Natl. Acad. Sci. U.S.A. 106, 3000-3005
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 3000-3005
    • Wu, P.1    Shui, W.2    Carlson, B.L.3    Hu, N.4    Rabuka, D.5    Lee, J.6    Bertozzi, C.R.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.