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Volumn 11, Issue 26, 2002, Pages 3319-3331

Functional requirements for fukutin-related protein in the Golgi apparatus

Author keywords

[No Author keywords available]

Indexed keywords

DYSTROGLYCAN; DYSTROPHIN; FUKUTIN; GLYCOSYLTRANSFERASE; ISOPROTEIN; MEMBRANE PROTEIN; MUSCLE PROTEIN; MUTANT PROTEIN; UNCLASSIFIED DRUG;

EID: 0037115482     PISSN: 09646906     EISSN: None     Source Type: Journal    
DOI: 10.1093/hmg/11.26.3319     Document Type: Review
Times cited : (118)

References (44)
  • 1
    • 0002315195 scopus 로고    scopus 로고
    • Congenital muscular dystrophies
    • Emery, A.E.H. (ed.), Oxford University Press, Oxford
    • Mercuri, E. and Muntoni, F. (2001) Congenital muscular dystrophies. In Emery, A.E.H. (ed.), The Muscular Dystrophies. Oxford University Press, Oxford, pp. 10-38.
    • (2001) The Muscular Dystrophies , pp. 10-38
    • Mercuri, E.1    Muntoni, F.2
  • 2
    • 0031934641 scopus 로고    scopus 로고
    • Congenital muscular dystrophies: 1997 update
    • Voit, T. (1998) Congenital muscular dystrophies: 1997 update. Brain Dev., 20, 65-74.
    • (1998) Brain Dev. , vol.20 , pp. 65-74
    • Voit, T.1
  • 3
    • 0034160119 scopus 로고    scopus 로고
    • The neurobiology of Duchenne muscular dystrophy: Learning lessons from muscle?
    • Blake, D.J. and Kroger, S. (2000) The neurobiology of Duchenne muscular dystrophy: learning lessons from muscle? Trends Neurosci., 23, 92-99.
    • (2000) Trends Neurosci. , vol.23 , pp. 92-99
    • Blake, D.J.1    Kroger, S.2
  • 5
    • 0036172254 scopus 로고    scopus 로고
    • The gene for a novel glycosyltransferase is mutated in congenital muscular dystrophy MDC1C and limb girdle muscular dystrophy 2I
    • Brockington, M., Blake, D.J., Brown, S.C. and Muntoni, F. (2002) The gene for a novel glycosyltransferase is mutated in congenital muscular dystrophy MDC1C and limb girdle muscular dystrophy 2I. Neuromuscul. Disord., 12, 233-234.
    • (2002) Neuromuscul. Disord. , vol.12 , pp. 233-234
    • Brockington, M.1    Blake, D.J.2    Brown, S.C.3    Muntoni, F.4
  • 7
    • 0031720377 scopus 로고    scopus 로고
    • Yayoi era mutation disrupts brain and muscle [news]
    • Eberhart, D.E. and Curran, T. (1998) Yayoi era mutation disrupts brain and muscle [news]. Nat. Med., 4, 1002-1003.
    • (1998) Nat. Med. , vol.4 , pp. 1002-1003
    • Eberhart, D.E.1    Curran, T.2
  • 8
    • 0019471880 scopus 로고
    • Congenital progressive muscular dystrophy of the Fukuyama type-clinical, genetic and pathological considerations
    • Fukuyama, Y., Osawa, M. and Suzuki, H. (1981) Congenital progressive muscular dystrophy of the Fukuyama type-clinical, genetic and pathological considerations. Brain Dev., 3, 1-29.
    • (1981) Brain Dev. , vol.3 , pp. 1-29
    • Fukuyama, Y.1    Osawa, M.2    Suzuki, H.3
  • 10
    • 0036087342 scopus 로고    scopus 로고
    • Function and genetics of dystrophin and dystrophin-related proteins in muscle
    • Blake, D.J., Weir, A., Newey, S.E. and Davies, K.E. (2002) Function and genetics of dystrophin and dystrophin-related proteins in muscle. Physiol. Rev., 82, 291-329.
    • (2002) Physiol. Rev. , vol.82 , pp. 291-329
    • Blake, D.J.1    Weir, A.2    Newey, S.E.3    Davies, K.E.4
  • 11
    • 0027458810 scopus 로고
    • Abnormal expression of dystrophin-associated proteins in Fukuyama-type congenital muscular dystrophy
    • [see comments]
    • Matsumura, K., Nonaka, I. and Campbell, K.P. (1993) Abnormal expression of dystrophin-associated proteins in Fukuyama-type congenital muscular dystrophy [see comments]. Lancet, 341, 521-522.
    • (1993) Lancet , vol.341 , pp. 521-522
    • Matsumura, K.1    Nonaka, I.2    Campbell, K.P.3
  • 12
    • 0035838362 scopus 로고    scopus 로고
    • Selective deficiency of alpha-dystroglycan in Fukuyama-type congenital muscular dystrophy
    • Hayashi, Y.K., Ogawa, M., Tagawa, K., Noguchi, S., Ishihara, T., Nonaka, I. and Arahata, K. (2001) Selective deficiency of alpha-dystroglycan in Fukuyama-type congenital muscular dystrophy. Neurology, 57, 115-121.
    • (2001) Neurology , vol.57 , pp. 115-121
    • Hayashi, Y.K.1    Ogawa, M.2    Tagawa, K.3    Noguchi, S.4    Ishihara, T.5    Nonaka, I.6    Arahata, K.7
  • 13
    • 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, D.J., Prandini, P., Brown, S.C., Torelli, S., Benson, M.A., Ponting, C.P., Estournet, B., Romero, N.B., Mercuri, E. 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    Benson, M.A.6    Ponting, C.P.7    Estournet, B.8    Romero, N.B.9    Mercuri, E.10
  • 15
    • 0034214277 scopus 로고    scopus 로고
    • A new locus for autosomal recessive limb-girdle muscular dystrophy in a large consanguineous Tunisian family maps to chromosome 19ql3.3
    • Driss, A., Amouri, R., Ben Hamida, C., Souilem, S., Gouider-Khouja, N., Ben Hamida, M. and Hentati, F. (2000) A new locus for autosomal recessive limb-girdle muscular dystrophy in a large consanguineous Tunisian family maps to chromosome 19ql3.3. Neuromuscul. Disord., 10, 240-246.
    • (2000) Neuromuscul. Disord. , vol.10 , pp. 240-246
    • Driss, A.1    Amouri, R.2    Ben Hamida, C.3    Souilem, S.4    Gouider-Khouja, N.5    Ben Hamida, M.6    Hentati, F.7
  • 16
    • 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, S.C., Torelli, S., Benson, M.A., Herrmann, R., Anderson, L.V., Bashir, R., Burgunder, J.M. 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    Benson, M.A.6    Herrmann, R.7    Anderson, L.V.8    Bashir, R.9    Burgunder, J.M.10
  • 17
    • 0033581949 scopus 로고    scopus 로고
    • The fukutin protein family-predicted enzymes modifying cell-surface molecules
    • Aravind, L. and Koonin, E.V. (1999) The fukutin protein family-predicted enzymes modifying cell-surface molecules. Curr. Biol., 9, R836-R837.
    • (1999) Curr. Biol. , vol.9
    • Aravind, L.1    Koonin, E.V.2
  • 18
    • 0034975777 scopus 로고    scopus 로고
    • Mutant glycosyltransferase and altered glycosylation of alpha-dystroglycan in the myodystrophy mouse
    • Grewal, P.K., Holzfeind, P.J., Bittner, R.E. and Hewitt, J.E. (2001) Mutant glycosyltransferase and altered glycosylation of alpha-dystroglycan in the myodystrophy mouse. Nat. Genet., 28,151-154.
    • (2001) Nat. Genet. , vol.28 , pp. 151-154
    • Grewal, P.K.1    Holzfeind, P.J.2    Bittner, R.E.3    Hewitt, J.E.4
  • 22
    • 0031040995 scopus 로고    scopus 로고
    • Golgi localization of glycosyltransferases: More questions than answers
    • Colley, K.J. (1997) Golgi localization of glycosyltransferases: more questions than answers. Glycobiology, 7, 1-13.
    • (1997) Glycobiology , vol.7 , pp. 1-13
    • Colley, K.J.1
  • 23
    • 0033976679 scopus 로고    scopus 로고
    • Biosynthesis of dystroglycan: Processing of a precursor propeptide
    • Holt, K.H., Crosbie, R.H., Venzke, D.P. and Campbell, K.P. (2000) Biosynthesis of dystroglycan: processing of a precursor propeptide. FEBS Lett., 468, 79-83.
    • (2000) FEBS Lett. , vol.468 , pp. 79-83
    • Holt, K.H.1    Crosbie, R.H.2    Venzke, D.P.3    Campbell, K.P.4
  • 24
    • 0032584665 scopus 로고    scopus 로고
    • A common motif of eukaryotic glycosyltransferases is essential for the enzyme activity of large clostridial cytotoxins
    • Busch, C., Hofmann, F., Selzer, J., Munro, S., Jeckel, D. and Aktories, K. (1998) A common motif of eukaryotic glycosyltransferases is essential for the enzyme activity of large clostridial cytotoxins. J. Biol. Chem., 273, 19566-19572.
    • (1998) J. Biol. Chem. , vol.273 , pp. 19566-19572
    • Busch, C.1    Hofmann, F.2    Selzer, J.3    Munro, S.4    Jeckel, D.5    Aktories, K.6
  • 25
    • 0032493440 scopus 로고    scopus 로고
    • Activity of the yeast MNN1 alpha-1,3-mannosyltransferase requires a motif conserved in many other families of glycosyltransferases
    • Wiggins, C.A. and Munro, S. (1998) Activity of the yeast MNN1 alpha-1,3-mannosyltransferase requires a motif conserved in many other families of glycosyltransferases. Proc. Natl Acad. Sci. USA, 95, 7945-7950.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 7945-7950
    • Wiggins, C.A.1    Munro, S.2
  • 26
    • 0344628712 scopus 로고    scopus 로고
    • Structure-function analysis of the UDP-N-acetyl-D-galactosamine:Poly-peptide N-acetylgalactosaminyltransferase. Essential residues lie in a predicted active site cleft resembling a lactose repressor fold
    • Hagen, F.K., Hazes, B., Raffo, R., deSa, D. and Tabak, L.A. (1999) Structure-function analysis of the UDP-N-acetyl-D-galactosamine:poly-peptide N-acetylgalactosaminyltransferase. Essential residues lie in a predicted active site cleft resembling a lactose repressor fold. J. Biol. Chem., 274, 6797-6803.
    • (1999) J. Biol. Chem. , vol.274 , pp. 6797-6803
    • Hagen, F.K.1    Hazes, B.2    Raffo, R.3    deSa, D.4    Tabak, L.A.5
  • 27
    • 0034644110 scopus 로고    scopus 로고
    • The notch signalling regulator fringe acts in the Golgi apparatus and requires the glycosyltransferase signature motif DXD
    • Munro, S. and Freeman, M. (2000) The notch signalling regulator fringe acts in the Golgi apparatus and requires the glycosyltransferase signature motif DXD. Curr Biol., 10, 813-820.
    • (2000) Curr. Biol. , vol.10 , pp. 813-820
    • Munro, S.1    Freeman, M.2
  • 28
    • 0035260226 scopus 로고    scopus 로고
    • A glycomic approach to the identification and characterization of glycoprotein function in cells transfected with glycosyltransferase genes
    • Taniguchi, N., Ekuni, A., Ko, J.H., Miyoshi, E., Ikeda, Y., Ihara, Y., Nishikawa, A., Henke, K. and Takahashi, M. (2001) A glycomic approach to the identification and characterization of glycoprotein function in cells transfected with glycosyltransferase genes. Proteomics, 1, 239 247.
    • (2001) Proteomics , vol.1 , pp. 239-247
    • Taniguchi, N.1    Ekuni, A.2    Ko, J.H.3    Miyoshi, E.4    Ikeda, Y.5    Ihara, Y.6    Nishikawa, A.7    Henke, K.8    Takahashi, M.9
  • 30
    • 0032929524 scopus 로고    scopus 로고
    • Mannosylphosphate transfer to yeast mannan
    • 1426
    • Jigami, Y. and Odani, T. (1999) Mannosylphosphate transfer to yeast mannan. Biochim. Biophys. Acta, 1426, 335-345.
    • (1999) Biochim. Biophys. Acta , pp. 335-345
    • Jigami, Y.1    Odani, T.2
  • 31
    • 0030475074 scopus 로고    scopus 로고
    • Cloning and analysis of the MNN4 gene required for phosphorylation of N-linked oligosaccharides in Saccharomyces cerevisiae
    • Odani, T., Shimma, Y., Tanaka, A. and Jigami, Y. (1996) Cloning and analysis of the MNN4 gene required for phosphorylation of N-linked oligosaccharides in Saccharomyces cerevisiae. Glycobiology, 6, 805-810.
    • (1996) Glycobiology , vol.6 , pp. 805-810
    • Odani, T.1    Shimma, Y.2    Tanaka, A.3    Jigami, Y.4
  • 32
    • 0031590758 scopus 로고    scopus 로고
    • Mannosylphosphate transfer to cell wall mannan is regulated by the transcriptional level of the MNN4 gene in Saccharomyces cerevisiae
    • Odani, T., Shimma, Y., Wang, X.H, and Jigami, Y. (1997) Mannosylphosphate transfer to cell wall mannan is regulated by the transcriptional level of the MNN4 gene in Saccharomyces cerevisiae. FEBS Lett., 420, 186-190.
    • (1997) FEBS Lett. , vol.420 , pp. 186-190
    • Odani, T.1    Shimma, Y.2    Wang, X.H.3    Jigami, Y.4
  • 34
    • 0035252649 scopus 로고    scopus 로고
    • The complexities of dystroglycan
    • Winder, S.J. (2001) The complexities of dystroglycan. Trends Biochem. Sci., 26, 118-124.
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 118-124
    • Winder, S.J.1
  • 35
    • 0027275643 scopus 로고
    • A role for the dystrophin-glycoprotein complex as a transmembrane linker between laminin and actin
    • Ervasti, J.M. and Campbell, K.P. (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
  • 36
    • 0028178082 scopus 로고
    • Dystroglycan-alpha, a dystrophin-associated glycoprotein, is a functional agrin receptor
    • Gee, S.H., Montanaro, E, Lindenbaum, M.H. and Carbonetto, S. (1994) Dystroglycan-alpha, a dystrophin-associated glycoprotein, is a functional agrin receptor. Cell, 77, 675-686.
    • (1994) Cell , vol.77 , pp. 675-686
    • Gee, S.H.1    Montanaro, E.2    Lindenbaum, M.H.3    Carbonetto, S.4
  • 37
    • 0027941192 scopus 로고
    • Dystroglycan binds nerve and muscle agrin
    • Sugiyama, J., Bowen, D.C. and Hall, Z.W. (1994) Dystroglycan binds nerve and muscle agrin. Neuron, 13, 103-115.
    • (1994) Neuron , vol.13 , pp. 103-115
    • Sugiyama, J.1    Bowen, D.C.2    Hall, Z.W.3
  • 39
    • 0032855087 scopus 로고    scopus 로고
    • Fukuyama-type congenital muscular dystrophy: Close relation between changes in the muscle basal lamina and plasma membrane
    • [In Process Citation]
    • Matsubara, S., Mizuno, Y., Kitaguchi, T., Isozaki, E., Miyamoto, K. and Hirai, S. (1999) Fukuyama-type congenital muscular dystrophy: close relation between changes in the muscle basal lamina and plasma membrane [In Process Citation]. Neuromuscul. Disord., 9, 388-398.
    • (1999) Neuromuscul. Disord. , vol.9 , pp. 388-398
    • Matsubara, S.1    Mizuno, Y.2    Kitaguchi, T.3    Isozaki, E.4    Miyamoto, K.5    Hirai, S.6
  • 40
    • 0033401031 scopus 로고    scopus 로고
    • Fukuyama-type congenital muscular dystrophy: The first human disease to be caused by an ancient retrotransposal integration
    • Toda, T. and Kobayashi, K. (1999) Fukuyama-type congenital muscular dystrophy: the first human disease to be caused by an ancient retrotransposal integration. J. Mol. Med., 77, 816-823.
    • (1999) J. Mol. Med. , vol.77 , pp. 816-823
    • Toda, T.1    Kobayashi, K.2
  • 41
    • 0026607683 scopus 로고
    • Golgi retention of a trans-Golgi membrane protein, galactosyltransferase, requires cysteine and histidine residues within the membrane-anchoring domain
    • Aoki, D., Lee, N., Yamaguchi, N., Dubois, C. and Fukuda, M.N. (1992) Golgi retention of a trans-Golgi membrane protein, galactosyltransferase, requires cysteine and histidine residues within the membrane-anchoring domain. Proc. Natl Acad. Sci. USA, 89, 4319-4323.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 4319-4323
    • Aoki, D.1    Lee, N.2    Yamaguchi, N.3    Dubois, C.4    Fukuda, M.N.5
  • 42
    • 0029067675 scopus 로고
    • Golgi retention mechanism of beta-1,4-galactosyltransferase. Membrane-spanning domain-dependent homodimerization and association with alpha- and beta-tubulins
    • Yamaguchi, N. and Fukuda, M.N. (1995) Golgi retention mechanism of beta-1,4-galactosyltransferase. Membrane-spanning domain-dependent homodimerization and association with alpha- and beta-tubulins. J. Biol. Chem., 270, 12170-12176.
    • (1995) J. Biol. Chem. , vol.270 , pp. 12170-12176
    • Yamaguchi, N.1    Fukuda, M.N.2
  • 44
    • 0033230437 scopus 로고    scopus 로고
    • Different dystrophin-like complexes are expressed in neurons and glia
    • Blake, D.J., Hawkes, R., Benson, M.A. and Beesley, P.W. (1999) Different dystrophin-like complexes are expressed in neurons and glia. J. Cell Biol., 147, 645-658.
    • (1999) J. Cell Biol. , vol.147 , pp. 645-658
    • Blake, D.J.1    Hawkes, R.2    Benson, M.A.3    Beesley, P.W.4


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