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Volumn 6, Issue 8, 2011, Pages

Fukutin-related protein resides in the Golgi cisternae of skeletal muscle fibres and forms disulfide-linked homodimers via an N-terminal interaction

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA DYSTROGLYCAN; AMINO TERMINAL TELOPEPTIDE; CYSTEINE; DISULFIDE; FUKUTIN RELATED PROTEIN; HOMODIMER; BIOLOGICAL MARKER; CYSTEINE RICH FIBROBLAST GROWTH FACTOR RECEPTOR; CYSTEINE-RICH FIBROBLAST GROWTH FACTOR RECEPTOR; DITHIOTHREITOL; FIBROBLAST GROWTH FACTOR RECEPTOR; FKRP PROTEIN, HUMAN; MANNOSE; MULTIPROTEIN COMPLEX; OLIGOSACCHARIDE; PROTEIN; RECOMBINANT PROTEIN; SIALOGLYCOPROTEIN;

EID: 80052019442     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0022968     Document Type: Article
Times cited : (32)

References (46)
  • 1
    • 33645366723 scopus 로고    scopus 로고
    • Mechanisms of disease: congenital muscular dystrophies- glycosylation takes center stage
    • Martin PT, (2006) Mechanisms of disease: congenital muscular dystrophies- glycosylation takes center stage. Nat Clin Pract Neurol 2: 222-230.
    • (2006) Nat Clin Pract Neurol , vol.2 , pp. 222-230
    • Martin, P.T.1
  • 2
    • 33750070428 scopus 로고    scopus 로고
    • The genetic and molecular basis of muscular dystrophy: roles of cell-matrix linkage in the pathogenesis
    • Kanagawa M, Toda T, (2006) The genetic and molecular basis of muscular dystrophy: roles of cell-matrix linkage in the pathogenesis. J Hum Genet 51: 915-926.
    • (2006) J Hum Genet , vol.51 , pp. 915-926
    • Kanagawa, M.1    Toda, T.2
  • 3
    • 32244440192 scopus 로고    scopus 로고
    • Dystroglycan: from biosynthesis to pathogenesis of human disease
    • Barresi R, Campbell KP, (2006) Dystroglycan: from biosynthesis to pathogenesis of human disease. J Cell Sci 119: 199-207.
    • (2006) J Cell Sci , vol.119 , pp. 199-207
    • Barresi, R.1    Campbell, K.P.2
  • 5
    • 0025815479 scopus 로고
    • Membrane organization of the dystrophin- glycoprotein complex
    • Ervasti JM, Campbell KP, (1991) Membrane organization of the dystrophin- glycoprotein complex. Cell 66: 1121-1131.
    • (1991) Cell , vol.66 , pp. 1121-1131
    • Ervasti, J.M.1    Campbell, K.P.2
  • 6
    • 0027275643 scopus 로고
    • A role for the dystrophin-glycoprotein complex as a transmembrane linker between laminin and actin
    • Ervasti JM, Campbell KP, (1993) A role for the dystrophin-glycoprotein complex as a transmembrane linker between laminin and actin. J Cell Biol 122: 809-823.
    • (1993) J Cell Biol , vol.122 , pp. 809-823
    • Ervasti, J.M.1    Campbell, K.P.2
  • 7
    • 0037173670 scopus 로고    scopus 로고
    • Post-translational disruption of dystroglycan-ligand interactions in congenital muscular dystrophies
    • Michele DE, Barresi R, Kanagawa M, Saito F, Cohn RD, et al. (2002) Post-translational disruption of dystroglycan-ligand interactions in congenital muscular dystrophies. Nature 418: 417-422.
    • (2002) Nature , vol.418 , pp. 417-422
    • Michele, D.E.1    Barresi, R.2    Kanagawa, M.3    Saito, F.4    Cohn, R.D.5
  • 8
    • 18044400450 scopus 로고    scopus 로고
    • Molecular dystrophy and neural migration disorder caused by mutations in a glycosyltransferase, POMGnT1
    • Yoshida A, Kobayashi K, Manya H, Taniguchi K, Kano H, et al. (2001) Molecular dystrophy and neural migration disorder caused by mutations in a glycosyltransferase, POMGnT1. Dev Cell 5: 717-724.
    • (2001) Dev Cell , vol.5 , pp. 717-724
    • Yoshida, A.1    Kobayashi, K.2    Manya, H.3    Taniguchi, K.4    Kano, H.5
  • 9
    • 0038392675 scopus 로고    scopus 로고
    • Loss-of-function of an N-acetylglucosaminyltransferase, POMGnT1, in muscle-eye-brain disease
    • Manya H, Sakai K, Kobayashi K, Taniguchi K, Kawakita M, et al. (2003) Loss-of-function of an N-acetylglucosaminyltransferase, POMGnT1, in muscle-eye-brain disease. Biochem Biophys Res Commun 306: 93-97.
    • (2003) Biochem Biophys Res Commun , vol.306 , pp. 93-97
    • Manya, H.1    Sakai, K.2    Kobayashi, K.3    Taniguchi, K.4    Kawakita, M.5
  • 10
    • 0038185363 scopus 로고    scopus 로고
    • Mutations in the O-mannosyltransferase gene POMT1 give rise to the severe neuronal migration disorder Walker-Warburg syndrome
    • Beltrán-Valero de Bernabé D, Currier S, Steinbrecher A, Celli J, van Beusekom E, et al. (2002) Mutations in the O-mannosyltransferase gene POMT1 give rise to the severe neuronal migration disorder Walker-Warburg syndrome. Am J Hum Genet 71: 1033-1043.
    • (2002) Am J Hum Genet , vol.71 , pp. 1033-1043
    • Beltrán-Valero de Bernabé, D.1    Currier, S.2    Steinbrecher, A.3    Celli, J.4    van Beusekom, E.5
  • 11
    • 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, et al. (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
  • 13
    • 10744226857 scopus 로고    scopus 로고
    • Mutations in the human LARGE gene cause MDC1D, a novel form of congenital muscular dystrophy with severe mental retardation and abnormal glycosylation of alpha-dystroglycan
    • Longman C, Brockington M, Torelli S, Jimenez-Mallebrera C, Kennedy C, et al. (2003) Mutations in the human LARGE gene cause MDC1D, a novel form of congenital muscular dystrophy with severe mental retardation and abnormal glycosylation of alpha-dystroglycan. Hum Mol Genet 12: 2853-2861.
    • (2003) Hum Mol Genet , vol.12 , pp. 2853-2861
    • Longman, C.1    Brockington, M.2    Torelli, S.3    Jimenez-Mallebrera, C.4    Kennedy, C.5
  • 14
    • 74849131820 scopus 로고    scopus 로고
    • O-mannosyl phosphorylation of alpha-dystroglycan is required for laminin binding
    • Yoshida-Moriguchi T, Yu L, Stalnaker SH, Davis S, Kunz S, et al. (2010) O-mannosyl phosphorylation of alpha-dystroglycan is required for laminin binding. Science 327: 88-92.
    • (2010) Science , vol.327 , pp. 88-92
    • Yoshida-Moriguchi, T.1    Yu, L.2    Stalnaker, S.H.3    Davis, S.4    Kunz, S.5
  • 15
    • 0032560851 scopus 로고    scopus 로고
    • An ancient retrotransposal insertion causes Fukuyama-type congenital muscular dystrophy
    • Kobayashi K, Nakahori Y, Miyake M, Matsumura K, Kondo-lida E, et al. (1998) An ancient retrotransposal insertion causes Fukuyama-type congenital muscular dystrophy. Nature 394: 388-392.
    • (1998) Nature , vol.394 , pp. 388-392
    • Kobayashi, K.1    Nakahori, Y.2    Miyake, M.3    Matsumura, K.4    Kondo-lida, E.5
  • 16
    • 0033581949 scopus 로고    scopus 로고
    • The fukutin protein family - predicted enzymes modifying cell-surface molecules
    • Aravind L, Koonin EV, (1999) The fukutin protein family- predicted enzymes modifying cell-surface molecules. Curr Biol 9: R836-837.
    • (1999) Curr Biol , vol.9 , pp. 836-837
    • Aravind, L.1    Koonin, E.V.2
  • 17
    • 0035212037 scopus 로고    scopus 로고
    • Mutations in the fukutin-related protein gene (FKRP) cause a form of congenital muscular dystrophy with secondary laminin alpha2 deficiency and abnormal glycosylation of alpha-dystroglycan
    • Brockington M, Blake DJ, Prandini P, Brown SC, Torelli S, et al. (2001) Mutations in the fukutin-related protein gene (FKRP) cause a form of congenital muscular dystrophy with secondary laminin alpha2 deficiency and abnormal glycosylation of alpha-dystroglycan. Am J Hum Genet 69: 1198-1209.
    • (2001) Am J Hum Genet , vol.69 , pp. 1198-1209
    • Brockington, M.1    Blake, D.J.2    Prandini, P.3    Brown, S.C.4    Torelli, S.5
  • 18
    • 18244375299 scopus 로고    scopus 로고
    • Mutations in the fukutin-related protein gene (FKRP) identify limb girdle muscular dystrophy 2I as a milder allelic variant of congenital muscular dystrophy MDC1C
    • Brockington M, Yuva Y, Prandini P, Brown SC, Torelli S, et al. (2001) Mutations in the fukutin-related protein gene (FKRP) identify limb girdle muscular dystrophy 2I as a milder allelic variant of congenital muscular dystrophy MDC1C. Hum Mol Genet 10: 2851-2859.
    • (2001) Hum Mol Genet , vol.10 , pp. 2851-2859
    • Brockington, M.1    Yuva, Y.2    Prandini, P.3    Brown, S.C.4    Torelli, S.5
  • 19
    • 3042850663 scopus 로고    scopus 로고
    • Mutations in the FKRP gene can cause muscle-eye-brain disease and Walker-Warburg syndrome
    • Available, Accessed 2011 Feb 5
    • Beltran-Valero de Bernabé D, Voit T, Longman C, Steinbrecher A, Straub V, et al. (2004) Mutations in the FKRP gene can cause muscle-eye-brain disease and Walker-Warburg syndrome. J Med Genet 2004;41: e61 Available: (http://www.jmedgenet.com/cgi/content/full/41/5/e61). Accessed 2011 Feb 5.
    • (2004) J Med Genet 2004 , vol.41
    • Beltran-Valero de Bernabé, D.1    Voit, T.2    Longman, C.3    Steinbrecher, A.4    Straub, V.5
  • 20
    • 10744223007 scopus 로고    scopus 로고
    • New FKRP mutations causing congenital muscular dystrophy associated with mental retardation and central nervous system abnormalities. Identification of a founder mutation in Tunisian families
    • Louhichi N, Triki C, Quijano-Roy S, Richard P, Makri S, et al. (2004) New FKRP mutations causing congenital muscular dystrophy associated with mental retardation and central nervous system abnormalities. Identification of a founder mutation in Tunisian families. Neurogenetics 5: 27-34.
    • (2004) Neurogenetics , vol.5 , pp. 27-34
    • Louhichi, N.1    Triki, C.2    Quijano-Roy, S.3    Richard, P.4    Makri, S.5
  • 21
    • 69949154343 scopus 로고    scopus 로고
    • A comparative study of alpha-dystroglycan glycosylation in dystroglycanopathies suggests that the hypoglycosylation of alpha-dystroglycan does not consistently correlate with clinical severity
    • Jimenez-Mallebrera C, Torelli S, Feng L, Kim J, Godfrey C, (2009) A comparative study of alpha-dystroglycan glycosylation in dystroglycanopathies suggests that the hypoglycosylation of alpha-dystroglycan does not consistently correlate with clinical severity. Brain Pathol 19: 596-611.
    • (2009) Brain Pathol , vol.19 , pp. 596-611
    • Jimenez-Mallebrera, C.1    Torelli, S.2    Feng, L.3    Kim, J.4    Godfrey, C.5
  • 22
    • 0037388120 scopus 로고    scopus 로고
    • Protein glycosylation in disease: new insights into the congenital muscular dystrophies
    • Martin-Rendon E, Blake DJ, (2003) Protein glycosylation in disease: new insights into the congenital muscular dystrophies. Trends Pharmacol Sci 24: 178-83.
    • (2003) Trends Pharmacol Sci , vol.24 , pp. 178-183
    • Martin-Rendon, E.1    Blake, D.J.2
  • 23
    • 76749117489 scopus 로고    scopus 로고
    • How do nematodes transfer phosphorylcholine to carbohydrates?
    • Harnett W, Rzepecka J, Houston KM, (2010) How do nematodes transfer phosphorylcholine to carbohydrates? Trends Parasitol 26: 114-118.
    • (2010) Trends Parasitol , vol.26 , pp. 114-118
    • Harnett, W.1    Rzepecka, J.2    Houston, K.M.3
  • 24
    • 3142628122 scopus 로고    scopus 로고
    • Subcellular localization of fukutin and fukutin-related protein in muscle cells
    • Matsumoto H, Noguchi S, Sugie K, Ogawa M, Murayama K, et al. (2004) Subcellular localization of fukutin and fukutin-related protein in muscle cells. J Biochem 135: 709-712.
    • (2004) J Biochem , vol.135 , pp. 709-712
    • Matsumoto, H.1    Noguchi, S.2    Sugie, K.3    Ogawa, M.4    Murayama, K.5
  • 25
    • 28244500576 scopus 로고    scopus 로고
    • Sub-cellular localisation of fukutin related protein in different cell lines and in the muscle of patients with MDC1C and LGMD2I
    • Torelli S, Brown SC, Brockington M, Dolatshad NF, Jimenez C, et al. (2005) Sub-cellular localisation of fukutin related protein in different cell lines and in the muscle of patients with MDC1C and LGMD2I. Neuromuscul Disord 15: 836-843.
    • (2005) Neuromuscul Disord , vol.15 , pp. 836-843
    • Torelli, S.1    Brown, S.C.2    Brockington, M.3    Dolatshad, N.F.4    Jimenez, C.5
  • 27
    • 12744279620 scopus 로고    scopus 로고
    • Fukutin-related protein mutations that cause congenital muscular dystrophy result in ER-retention of the mutant protein in cultured cells
    • Esapa CT, McIlhinney RA, Blake DJ, (2005) Fukutin-related protein mutations that cause congenital muscular dystrophy result in ER-retention of the mutant protein in cultured cells. Hum Mol Genet 14: 295-305.
    • (2005) Hum Mol Genet , vol.14 , pp. 295-305
    • Esapa, C.T.1    McIlhinney, R.A.2    Blake, D.J.3
  • 28
    • 24944439901 scopus 로고    scopus 로고
    • Mutated fukutin-related protein (FKRP) localises as wild type in differentiated muscle cells
    • Dolatshad NF, Brockington M, Torelli S, Skordis L, Wever U, et al. (2005) Mutated fukutin-related protein (FKRP) localises as wild type in differentiated muscle cells. Exp Cell Res 309: 370-378.
    • (2005) Exp Cell Res , vol.309 , pp. 370-378
    • Dolatshad, N.F.1    Brockington, M.2    Torelli, S.3    Skordis, L.4    Wever, U.5
  • 29
    • 34848836665 scopus 로고    scopus 로고
    • Fukutin-related protein localizes to the Golgi apparatus and mutations lead to mislocalization in muscle in vivo
    • Keramaris-Vrantsis E, Lu PJ, Doran T, Zillmer A, Ashar J, et al. (2007) Fukutin-related protein localizes to the Golgi apparatus and mutations lead to mislocalization in muscle in vivo. Muscle Nerve 36: 455-465.
    • (2007) Muscle Nerve , vol.36 , pp. 455-465
    • Keramaris-Vrantsis, E.1    Lu, P.J.2    Doran, T.3    Zillmer, A.4    Ashar, J.5
  • 31
    • 34447123225 scopus 로고    scopus 로고
    • Fukutin-related protein associates with the sarcolemmal dystrophin-glycoprotein complex
    • Beedle AM, Nienaber PM, Campbell KP, (2007) Fukutin-related protein associates with the sarcolemmal dystrophin-glycoprotein complex. J Biol Chem 282: 16713-16717.
    • (2007) J Biol Chem , vol.282 , pp. 16713-16717
    • Beedle, A.M.1    Nienaber, P.M.2    Campbell, K.P.3
  • 32
    • 0033573371 scopus 로고    scopus 로고
    • The organization of the Golgi complex and microtubules in skeletal muscle is fiber type-dependent
    • Ralston E, Lu Z, Ploug T, (1999) The organization of the Golgi complex and microtubules in skeletal muscle is fiber type-dependent. J Neurosci 19: 10694-10705.
    • (1999) J Neurosci , vol.19 , pp. 10694-10705
    • Ralston, E.1    Lu, Z.2    Ploug, T.3
  • 33
    • 0031809680 scopus 로고    scopus 로고
    • Targeting of proteins to the Golgi apparatus
    • Gleeson PA, (1998) Targeting of proteins to the Golgi apparatus. Histochem Cell Biol 109: 517-532.
    • (1998) Histochem Cell Biol , vol.109 , pp. 517-532
    • Gleeson, P.A.1
  • 34
    • 0034838654 scopus 로고    scopus 로고
    • Structural and functional features of glycosyltransferases
    • Breton C, Mucha J, Jeanneau C, (2001) Structural and functional features of glycosyltransferases. Biochimie 83: 713-718.
    • (2001) Biochimie , vol.83 , pp. 713-718
    • Breton, C.1    Mucha, J.2    Jeanneau, C.3
  • 35
    • 0344237268 scopus 로고    scopus 로고
    • Different glycosyltransferases are differentially processed for secretion, dimerization, and autoglycosylation
    • El-Battari A, Prorok M, Angata K, Mathieu S, Zerfaoui M, et al. (2003) Different glycosyltransferases are differentially processed for secretion, dimerization, and autoglycosylation. Glycobiology 13: 941-953.
    • (2003) Glycobiology , vol.13 , pp. 941-953
    • El-Battari, A.1    Prorok, M.2    Angata, K.3    Mathieu, S.4    Zerfaoui, M.5
  • 36
    • 77952944920 scopus 로고    scopus 로고
    • Golgi N-glycosyltransferases form both homo- and heterodimeric complexes in live cells
    • Hassinen A, Rivinoja A, Kauppila A, Kellokumpu S, (2010) Golgi N-glycosyltransferases form both homo- and heterodimeric complexes in live cells. J Biol Chem 285: 17771-17777.
    • (2010) J Biol Chem , vol.285 , pp. 17771-17777
    • Hassinen, A.1    Rivinoja, A.2    Kauppila, A.3    Kellokumpu, S.4
  • 37
    • 3142514373 scopus 로고    scopus 로고
    • The roles of enzyme localisation and complex formation in glycan assembly within the Golgi apparatus
    • de Graffenried CL, Bertozzi CR, (2004) The roles of enzyme localisation and complex formation in glycan assembly within the Golgi apparatus. Curr Opin Cell Biol 16: 356-363.
    • (2004) Curr Opin Cell Biol , vol.16 , pp. 356-363
    • de Graffenried, C.L.1    Bertozzi, C.R.2
  • 38
    • 1642404941 scopus 로고    scopus 로고
    • Organization of Golgi glycosyltransferases in membranes: complexity via complexes
    • Young WW Jr, (2004) Organization of Golgi glycosyltransferases in membranes: complexity via complexes. J Membr Biol 198: 1-13.
    • (2004) J Membr Biol , vol.198 , pp. 1-13
    • Young Jr., W.W.1
  • 39
    • 0035499236 scopus 로고    scopus 로고
    • Localization of sarcoglycan, neuronal nitric oxide synthase, beta-dystroglycan, and dystrophin molecules in normal skeletal myofiber: triple immunogold labeling electron microscopy
    • Wakayama Y, Inoue M, Kojima H, Murahashi M, Shibuya S, et al. (2001) Localization of sarcoglycan, neuronal nitric oxide synthase, beta-dystroglycan, and dystrophin molecules in normal skeletal myofiber: triple immunogold labeling electron microscopy. Microsc Res Tech 55: 154-163.
    • (2001) Microsc Res Tech , vol.55 , pp. 154-163
    • Wakayama, Y.1    Inoue, M.2    Kojima, H.3    Murahashi, M.4    Shibuya, S.5
  • 40
    • 0031876030 scopus 로고    scopus 로고
    • Co-localization of dystrophin and beta-dystroglycan demonstrated in en face view by double immunogold labeling of freeze-fractured skeletal muscle
    • Cullen MJ, Walsh J, Stevenson SA, Rothery S, Severs NJ, (1998) Co-localization of dystrophin and beta-dystroglycan demonstrated in en face view by double immunogold labeling of freeze-fractured skeletal muscle. J Histochem Cytochem 46: 945-954.
    • (1998) J Histochem Cytochem , vol.46 , pp. 945-954
    • Cullen, M.J.1    Walsh, J.2    Stevenson, S.A.3    Rothery, S.4    Severs, N.J.5
  • 41
    • 0031034587 scopus 로고    scopus 로고
    • Protein disulfide isomerase and newly synthesized procollagen chains form higher-order structures in the lumen of the endoplasmic reticulum
    • Kellokumpu S, Suokas M, Risteli L, Myllylä R, (1997) Protein disulfide isomerase and newly synthesized procollagen chains form higher-order structures in the lumen of the endoplasmic reticulum. J Biol Chem 272: 2770-2777.
    • (1997) J Biol Chem , vol.272 , pp. 2770-2777
    • Kellokumpu, S.1    Suokas, M.2    Risteli, L.3    Myllylä, R.4
  • 42
    • 84985180850 scopus 로고
    • Application of cryoultramicrotomy to immunocytochemistry
    • Tokuyasu KT, (1986) Application of cryoultramicrotomy to immunocytochemistry. J Microsc 143: 139-149.
    • (1986) J Microsc , vol.143 , pp. 139-149
    • Tokuyasu, K.T.1
  • 44
    • 0029099409 scopus 로고
    • Ras-Raf interaction: two-hybrid analysis
    • Vojtek A, Hollenberg SM, (1995) Ras-Raf interaction: two-hybrid analysis. Methods Enzymol 255: 331-342.
    • (1995) Methods Enzymol , vol.255 , pp. 331-342
    • Vojtek, A.1    Hollenberg, S.M.2
  • 46
    • 0030963019 scopus 로고    scopus 로고
    • Toward a functional analysis of the yeast genome through exhaustive two-hybrid screens
    • Fromont-Racine M, Rain JC, Legrain P, (1997) Toward a functional analysis of the yeast genome through exhaustive two-hybrid screens. Nat Genet 16: 277-282.
    • (1997) Nat Genet , vol.16 , pp. 277-282
    • Fromont-Racine, M.1    Rain, J.C.2    Legrain, P.3


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