메뉴 건너뛰기




Volumn 18, Issue 12, 2007, Pages 4721-4730

Dystroglycan and protein O-mannosyltransferases 1 and 2 are required to maintain integrity of Drosophila larval muscles

Author keywords

[No Author keywords available]

Indexed keywords

DYSTROGLYCAN; MANNOSE; MANNOSYLTRANSFERASE; MANNOSYLTRANSFERASE 1; MANNOSYLTRANSFERASE 2; UNCLASSIFIED DRUG;

EID: 37049002059     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.E07-01-0047     Document Type: Article
Times cited : (54)

References (44)
  • 1
    • 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
  • 2
    • 33745817404 scopus 로고    scopus 로고
    • Physical and functional association of human protein O-mannosyl-transferases 1 and 2
    • Akasaka-Manya, K., Manya, H., Nakajima, A., Kawakita, M., and Endo, T. (2006). Physical and functional association of human protein O-mannosyl-transferases 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
  • 3
    • 32244440192 scopus 로고    scopus 로고
    • Dystroglycan: From biosynthesis to pathogenesis of human disease
    • Barresi, R., and Campbell, K. P. (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
  • 4
    • 0025221554 scopus 로고
    • The embryonic development of larval muscles in Drosophila
    • Bate, M. (1990). The embryonic development of larval muscles in Drosophila. Development 110, 791-804.
    • (1990) Development , vol.110 , pp. 791-804
    • Bate, M.1
  • 5
    • 0032432922 scopus 로고    scopus 로고
    • Mutations in the Caenorhabditis elegans dystrophin-like gene dys-1 lead to hyperactivity and suggest a link with cholinergic transmission
    • Bessou, C., Giugia, J. B., Franks, C. J., Holden-Dye, L., and Segalat, L. (1998). Mutations in the Caenorhabditis elegans dystrophin-like gene dys-1 lead to hyperactivity and suggest a link with cholinergic transmission. Neurogenetics 2, 61-72.
    • (1998) Neurogenetics , vol.2 , pp. 61-72
    • Bessou, C.1    Giugia, J.B.2    Franks, C.J.3    Holden-Dye, L.4    Segalat, L.5
  • 6
    • 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
  • 7
    • 0028173625 scopus 로고
    • Null mutations in the alpha PS2 and beta PS integrin subunit genes have distinct phenotypes
    • Brown, N. H. (1994). Null mutations in the alpha PS2 and beta PS integrin subunit genes have distinct phenotypes. Development 120, 1221-1231.
    • (1994) Development , vol.120 , pp. 1221-1231
    • Brown, N.H.1
  • 8
    • 0031026624 scopus 로고    scopus 로고
    • Structures of sialylated O-linked oligosaccharides of bovine peripheral nerve alpha-dystroglycan. The role of a novel O-mannosyl-type oligosaccharide in the binding of alpha-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 alpha-dystroglycan. The role of a novel O-mannosyl-type oligosaccharide in the binding of alpha-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
  • 9
    • 23944504765 scopus 로고    scopus 로고
    • Enhanced laminin binding by alpha-dystroglycan after enzymatic deglycosylation
    • Combs, A. C., and Ervasti, J. M. (2005). Enhanced laminin binding by alpha-dystroglycan after enzymatic deglycosylation. Biochem. J. 390, 303-309.
    • (2005) Biochem. J , vol.390 , pp. 303-309
    • Combs, A.C.1    Ervasti, J.M.2
  • 10
    • 0016425461 scopus 로고
    • Stages in fibre breakdown in Duchenne muscular dystrophy. An electron-microscopic study
    • Cullen, M. J., and Fulthorpe, J. J. (1975). Stages in fibre breakdown in Duchenne muscular dystrophy. An electron-microscopic study. J. Neurol. Sci. 24, 179-200.
    • (1975) J. Neurol. Sci , vol.24 , pp. 179-200
    • Cullen, M.J.1    Fulthorpe, J.J.2
  • 11
    • 0031017192 scopus 로고    scopus 로고
    • Electrical properties of diaphragm and EDL muscles during the life of dystrophic mice
    • De Luca, A., Pierno, S., and Camerino, D. C. (1997). Electrical properties of diaphragm and EDL muscles during the life of dystrophic mice. Am. J. Physiol. 272, C333-C340.
    • (1997) Am. J. Physiol , vol.272
    • De Luca, A.1    Pierno, S.2    Camerino, D.C.3
  • 12
    • 33947258069 scopus 로고    scopus 로고
    • Pathophysiology of duchenne muscular dystrophy: Current hypotheses
    • Deconinck, N., and Dan, B. (2007). Pathophysiology of duchenne muscular dystrophy: current hypotheses. Pediatr. Neurol. 36, 1-7.
    • (2007) Pediatr. Neurol , vol.36 , pp. 1-7
    • Deconinck, N.1    Dan, B.2
  • 13
    • 0842279652 scopus 로고    scopus 로고
    • Dekkers, L. C., van der Plas, M. C., van Loenen, P. B., den Dunnen, J. T., van Ommen, G. J., Fradkin, L. G., and Noordermeer, J. N. (2004). Embryonic expression patterns of the Drosophila dystrophin-associated glycoprotein complex orthologs. Gene Expr. Patterns 4, 153-159.
    • Dekkers, L. C., van der Plas, M. C., van Loenen, P. B., den Dunnen, J. T., van Ommen, G. J., Fradkin, L. G., and Noordermeer, J. N. (2004). Embryonic expression patterns of the Drosophila dystrophin-associated glycoprotein complex orthologs. Gene Expr. Patterns 4, 153-159.
  • 14
    • 33846309701 scopus 로고    scopus 로고
    • Integrins and the actin cytoskeleton
    • Delon, I., and Brown, N. H. (2007). Integrins and the actin cytoskeleton. Curr. Opin. Cell Biol. 19, 43-50.
    • (2007) Curr. Opin. Cell Biol , vol.19 , pp. 43-50
    • Delon, I.1    Brown, N.H.2
  • 16
    • 0027712266 scopus 로고
    • Dystrophin-associated glycoproteins: Their possible roles in the pathogenesis of Duchenne muscular dystrophy
    • Ervasti, J. M., and Campbell, K. P. (1993). Dystrophin-associated glycoproteins: their possible roles in the pathogenesis of Duchenne muscular dystrophy. Mol. Cell Biol. Hum. Dis. Ser. 3, 139-166.
    • (1993) Mol. Cell Biol. Hum. Dis. Ser , vol.3 , pp. 139-166
    • Ervasti, J.M.1    Campbell, K.P.2
  • 17
    • 27144512277 scopus 로고    scopus 로고
    • Cardiac involvement in muscular dystrophies: Molecular mechanisms
    • Goodwin, F. C., and Muntoni, F. (2005). Cardiac involvement in muscular dystrophies: molecular mechanisms. Muscle Nerve 32, 577-588.
    • (2005) Muscle Nerve , vol.32 , pp. 577-588
    • Goodwin, F.C.1    Muntoni, F.2
  • 18
    • 0034730882 scopus 로고    scopus 로고
    • Conservation of components of the dystrophin complex in Drosophila
    • Greener, M. J., and Roberts, R. G. (2000). Conservation of components of the dystrophin complex in Drosophila. FEBS Lett. 482, 13-18.
    • (2000) FEBS Lett , vol.482 , pp. 13-18
    • Greener, M.J.1    Roberts, R.G.2
  • 19
    • 0037055258 scopus 로고    scopus 로고
    • Genetic evidence for a dystrophin-glycoprotein complex (DGC) in Caenorhabditis elegans
    • Grisoni, K., Martin, E., Gieseler, K., Mariol, M. C., and Segalat, L. (2002). Genetic evidence for a dystrophin-glycoprotein complex (DGC) in Caenorhabditis elegans. Gene 294, 77-86.
    • (2002) Gene , vol.294 , pp. 77-86
    • Grisoni, K.1    Martin, E.2    Gieseler, K.3    Mariol, M.C.4    Segalat, L.5
  • 20
    • 34247897153 scopus 로고    scopus 로고
    • Functional roles for β 1,4-N-acetlygalactosaminyltransferase-A in Drosophila larval neurons and muscles
    • Haines, N., and Stewart, B. A. (2007). Functional roles for β 1,4-N-acetlygalactosaminyltransferase-A in Drosophila larval neurons and muscles. Genetics 175, 671-679.
    • (2007) Genetics , vol.175 , pp. 671-679
    • Haines, N.1    Stewart, B.A.2
  • 21
    • 5644228696 scopus 로고    scopus 로고
    • The twisted abdomen phenotype of Drosophila POMT1 and POMT2 mutants coincides with their heterophilic protein O-mannosyltransferase activity
    • Ichimiya, T., Manya, H., Ohmae, Y., Yoshida, H., Takahashi, K., Ueda, R., Endo, T., and Nishihara, S. (2004). The twisted abdomen phenotype of Drosophila POMT1 and POMT2 mutants coincides with their heterophilic protein O-mannosyltransferase activity. J. Biol. Chem. 279, 42638-42647.
    • (2004) J. Biol. Chem , vol.279 , pp. 42638-42647
    • Ichimiya, T.1    Manya, H.2    Ohmae, Y.3    Yoshida, H.4    Takahashi, K.5    Ueda, R.6    Endo, T.7    Nishihara, S.8
  • 22
    • 33750070428 scopus 로고    scopus 로고
    • The genetic and molecular basis of muscular dystrophy: Roles of cell-matrix linkage in the pathogenesis
    • Kanagawa, M., and 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
  • 23
    • 0034612267 scopus 로고    scopus 로고
    • Distinct patterns of dystrophin organization in myocyte sarcolemma and transverse tubules of normal and diseased human myocardium
    • Kaprielian, R. R., Stevenson, S., Rothery, S. M., Cullen, M. J., and Severs, N. J. (2000). Distinct patterns of dystrophin organization in myocyte sarcolemma and transverse tubules of normal and diseased human myocardium. Circulation 101, 2586-2594.
    • (2000) Circulation , vol.101 , pp. 2586-2594
    • Kaprielian, R.R.1    Stevenson, S.2    Rothery, S.M.3    Cullen, M.J.4    Severs, N.J.5
  • 24
    • 0027533969 scopus 로고
    • Dystrophin-glycoprotein complex and laminin colocalize to the sarcolemma and transverse tubules of cardiac muscle
    • Klietsch, R., Ervasti, J. M., Arnold, W., Campbell, K. P., and Jorgensen, A. O. (1993). Dystrophin-glycoprotein complex and laminin colocalize to the sarcolemma and transverse tubules of cardiac muscle. Circ. Res. 72, 349-360.
    • (1993) Circ. Res , vol.72 , pp. 349-360
    • Klietsch, R.1    Ervasti, J.M.2    Arnold, W.3    Campbell, K.P.4    Jorgensen, A.O.5
  • 25
    • 2342621479 scopus 로고    scopus 로고
    • The dystrophin glycoprotein complex: Signaling strength and integrity for the sarcolemma
    • Lapidos, K. A., Kakkar, R., and McNaIIy, E. M. (2004). The dystrophin glycoprotein complex: signaling strength and integrity for the sarcolemma. Circ. Res. 94, 1023-1031.
    • (2004) Circ. Res , vol.94 , pp. 1023-1031
    • Lapidos, K.A.1    Kakkar, R.2    McNaIIy, E.M.3
  • 26
    • 33644768085 scopus 로고    scopus 로고
    • The twisted gene encodes Drosophila protein O-mannosyltransferase 2 and genetically interacts with the rotated abdomen gene encoding Drosophila protein O-mannosyltransferase 1
    • Lyalin, D., Koles, K., Roosendaal, S. D., Repnikova, E., Van Wechel, L., and Panin, V. M. (2006). The twisted gene encodes Drosophila protein O-mannosyltransferase 2 and genetically interacts with the rotated abdomen gene encoding Drosophila protein O-mannosyltransferase 1. Genetics 172, 343-353.
    • (2006) Genetics , vol.172 , pp. 343-353
    • Lyalin, D.1    Koles, K.2    Roosendaal, S.D.3    Repnikova, E.4    Van Wechel, L.5    Panin, V.M.6
  • 27
    • 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
  • 28
    • 0029973140 scopus 로고    scopus 로고
    • Mutations in the rotated abdomen locus affect muscle development and reveal an intrinsic asymmetry in Drosophila
    • Martin-Blanco, E., and Garcia-Bellido, A. (1996). Mutations in the rotated abdomen locus affect muscle development and reveal an intrinsic asymmetry in Drosophila. Proc. Natl. Acad. Sci. USA 93, 6048-6052.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 6048-6052
    • Martin-Blanco, E.1    Garcia-Bellido, A.2
  • 29
    • 0037173670 scopus 로고    scopus 로고
    • Post-translational disruption of dystroglycan-ligand interactions in congenital muscular dystrophies
    • Michele, D. E. 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
  • 30
    • 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
  • 31
  • 32
    • 0035941476 scopus 로고    scopus 로고
    • The dystrophin/utrophin homologues in Drosophila and in sea urchin
    • Neuman, S., Kaban, A., Volk, T., Yaffe, D., and Nudel, U. (2001). The dystrophin/utrophin homologues in Drosophila and in sea urchin. Gene 263, 17-29.
    • (2001) Gene , vol.263 , pp. 17-29
    • Neuman, S.1    Kaban, A.2    Volk, T.3    Yaffe, D.4    Nudel, U.5
  • 33
    • 33748073445 scopus 로고    scopus 로고
    • Dystroglycan down-regulation links EGF receptor signaling and anterior-posterior polarity formation in the Drosophila oocyte
    • Poulton, J. S., and Deng, W. M. (2006). Dystroglycan down-regulation links EGF receptor signaling and anterior-posterior polarity formation in the Drosophila oocyte. Proc. Natl. Acad. Sci. USA 103, 12775-12780.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 12775-12780
    • Poulton, J.S.1    Deng, W.M.2
  • 34
    • 0345055334 scopus 로고    scopus 로고
    • Absence of PS integrins or laminin A affects extracellular adhesion, but not intracellular assembly, of hemiadherens and neuromuscular junctions in Drosophila embryos
    • Prokop, A., Martin-Bermudo, M. D., Bate, M., and Brown, N. H. (1998). Absence of PS integrins or laminin A affects extracellular adhesion, but not intracellular assembly, of hemiadherens and neuromuscular junctions in Drosophila embryos. Dev. Biol. 196, 58-76.
    • (1998) Dev. Biol , vol.196 , pp. 58-76
    • Prokop, A.1    Martin-Bermudo, M.D.2    Bate, M.3    Brown, N.H.4
  • 35
    • 0035890136 scopus 로고    scopus 로고
    • Amphiphysin is necessary for organization of the excitation-contraction coupling machinery of muscles, but not for synaptic vesicle endocytosis in Drosophila
    • Razzaq, A., Robinson, I. M., McMahon, H. T., Skepper, J. N., Su, Y., Zelhof, A. C., Jackson, A. P., Gay, N. J., and O'Kane, C. J. (2001). Amphiphysin is necessary for organization of the excitation-contraction coupling machinery of muscles, but not for synaptic vesicle endocytosis in Drosophila. Genes Dev. 15, 2967-2979.
    • (2001) Genes Dev , vol.15 , pp. 2967-2979
    • Razzaq, A.1    Robinson, I.M.2    McMahon, H.T.3    Skepper, J.N.4    Su, Y.5    Zelhof, A.C.6    Jackson, A.P.7    Gay, N.J.8    O'Kane, C.J.9
  • 36
    • 33750469290 scopus 로고    scopus 로고
    • Perlecan and Dystroglycan act at the basal side of the Drosophila follicular epithelium to maintain epithelial organization
    • Schneider, M., Khalil, A. A., Poulton, J., Castillejo-Lopez, C., Egger-Adam, D., Wodarz, A., Deng, W. M., and Baumgartner, S. (2006). Perlecan and Dystroglycan act at the basal side of the Drosophila follicular epithelium to maintain epithelial organization. Development 133, 3805-3815.
    • (2006) Development , vol.133 , pp. 3805-3815
    • Schneider, M.1    Khalil, A.A.2    Poulton, J.3    Castillejo-Lopez, C.4    Egger-Adam, D.5    Wodarz, A.6    Deng, W.M.7    Baumgartner, S.8
  • 38
    • 0028483237 scopus 로고
    • Improved stability of Drosophila larval neuromuscular preparations in haemolymph-like physiological solutions
    • Stewart, B. A., Atwood, H. L., Renger, J. J., Wang, J., and Wu, C. F. (1994). Improved stability of Drosophila larval neuromuscular preparations in haemolymph-like physiological solutions. J. Comp. Physiol. [A] 175, 179-191.
    • (1994) J. Comp. Physiol , vol.175 , Issue.A , pp. 179-191
    • Stewart, B.A.1    Atwood, H.L.2    Renger, J.J.3    Wang, J.4    Wu, C.F.5
  • 39
    • 9144274057 scopus 로고    scopus 로고
    • Population density regulates Drosophila synaptic morphology in a Fasciclin-II-dependent manner
    • Stewart, B. A., and McLean, J. R. (2004). Population density regulates Drosophila synaptic morphology in a Fasciclin-II-dependent manner. J. Neurobiol. 61, 392-399.
    • (2004) J. Neurobiol , vol.61 , pp. 392-399
    • Stewart, B.A.1    McLean, J.R.2
  • 40
    • 30644469248 scopus 로고    scopus 로고
    • Dystrophin is required for appropriate retrograde control of neurotransmitter release at the Drosophila neuromuscular junction
    • van der Plas, M. C., Pilgram, G. S., Plomp, J. J., de Jong, A., Fradkin, L. G., and Noordermeer, J. N. (2006). Dystrophin is required for appropriate retrograde control of neurotransmitter release at the Drosophila neuromuscular junction. J. Neurosci. 26, 333-344.
    • (2006) J. Neurosci , vol.26 , pp. 333-344
    • van der Plas, M.C.1    Pilgram, G.S.2    Plomp, J.J.3    de Jong, A.4    Fradkin, L.G.5    Noordermeer, J.N.6
  • 41
    • 26944438148 scopus 로고    scopus 로고
    • POMT2 mutations cause alpha-dystroglycan hypoglycosylation and Walker-Warburg syndrome
    • van Reeuwijk, J. et al. (2005). POMT2 mutations cause alpha-dystroglycan hypoglycosylation and Walker-Warburg syndrome. J. Med. Genet. 42, 907-912.
    • (2005) J. Med. Genet , vol.42 , pp. 907-912
    • van Reeuwijk, J.1
  • 42
    • 0033230721 scopus 로고    scopus 로고
    • Singling out Drosophila tendon cells: A dialogue between two distinct cell types
    • Volk, T. (1999). Singling out Drosophila tendon cells: a dialogue between two distinct cell types. Trends Genet. 15, 448-453.
    • (1999) Trends Genet , vol.15 , pp. 448-453
    • Volk, T.1
  • 43
    • 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
  • 44
    • 0029004553 scopus 로고
    • Laminin is required for heart, somatic muscles, and gut development in the Drosophila embryo
    • Yarnitzky, T., and Volk, T. (1995). Laminin is required for heart, somatic muscles, and gut development in the Drosophila embryo. Dev. Biol. 169, 609-618.
    • (1995) Dev. Biol , vol.169 , pp. 609-618
    • Yarnitzky, T.1    Volk, T.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.