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Volumn 19, Issue 24, 2010, Pages 4820-4836

A centronuclear myopathy-dynamin 2 mutation impairs skeletal muscle structure and function in mice

Author keywords

[No Author keywords available]

Indexed keywords

DYNAMIN II; DYSFERLIN; UBIQUITIN;

EID: 78649471271     PISSN: 09646906     EISSN: 14602083     Source Type: Journal    
DOI: 10.1093/hmg/ddq413     Document Type: Article
Times cited : (97)

References (45)
  • 6
    • 77950930695 scopus 로고    scopus 로고
    • Centronuclear myopathies: a widening concept
    • Romero, N.B. (2010) Centronuclear myopathies: a widening concept. Neuromuscul. Disord., 20, 223-228.
    • (2010) Neuromuscul. Disord. , vol.20 , pp. 223-228
    • Romero, N.B.1
  • 10
    • 0028137796 scopus 로고
    • Identification of dynamin 2, an isoform ubiquitously expressed in rat tissues
    • Cook, T.A., Urrutia, R. and McNiven, M.A. (1994) Identification of dynamin 2, an isoform ubiquitously expressed in rat tissues. Proc. Natl Acad. Sci. USA, 91, 644-648.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 644-648
    • Cook, T.A.1    Urrutia, R.2    McNiven, M.A.3
  • 11
    • 0742288598 scopus 로고    scopus 로고
    • The dynamin superfamily: universal membrane tubulation and fission molecules?
    • Praefcke, G.J. and McMahon, H.T. (2004) The dynamin superfamily: universal membrane tubulation and fission molecules? Nat. Rev. Mol. Cell Biol., 5, 133-147.
    • (2004) Nat. Rev. Mol. Cell Biol. , vol.5 , pp. 133-147
    • Praefcke, G.J.1    McMahon, H.T.2
  • 14
    • 67449124363 scopus 로고    scopus 로고
    • Dynamic instability of microtubules requires dynamin 2 and is impaired in a Charcot-Marie-Tooth mutant
    • Tanabe, K. and Takei, K. (2009) Dynamic instability of microtubules requires dynamin 2 and is impaired in a Charcot-Marie-Tooth mutant. J. Cell Biol., 185, 939-48.
    • (2009) J. Cell Biol. , vol.185 , pp. 939-948
    • Tanabe, K.1    Takei, K.2
  • 16
    • 0041424822 scopus 로고    scopus 로고
    • Molecular mechanisms modulating muscle mass
    • Glass, D.J. (2003) Molecular mechanisms modulating muscle mass. Trends Mol. Med., 9, 344-350.
    • (2003) Trends Mol. Med. , vol.9 , pp. 344-350
    • Glass, D.J.1
  • 18
    • 33846015010 scopus 로고    scopus 로고
    • Rapid disuse and denervation atrophy involve transcriptional changes similar to those of muscle wasting during systemic diseases
    • Sacheck, J.M., Hyatt, J.P., Raffaello, A., Jagoe, R.T., Roy, R.R., Edgerton, V.R., Lecker, S.H. and Goldberg, A.L. (2007) Rapid disuse and denervation atrophy involve transcriptional changes similar to those of muscle wasting during systemic diseases. FASEB J., 21, 140-155.
    • (2007) FASEB J. , vol.21 , pp. 140-155
    • Sacheck, J.M.1    Hyatt, J.P.2    Raffaello, A.3    Jagoe, R.T.4    Roy, R.R.5    Edgerton, V.R.6    Lecker, S.H.7    Goldberg, A.L.8
  • 19
    • 49049083353 scopus 로고    scopus 로고
    • Signaling in muscle atrophy and hypertrophy
    • Sandri, M. (2008) Signaling in muscle atrophy and hypertrophy. Physiology (Bethesda), 23, 160-170.
    • (2008) Physiology (Bethesda) , vol.23 , pp. 160-170
    • Sandri, M.1
  • 22
    • 36448968532 scopus 로고    scopus 로고
    • FoxO3 coordinately activates protein degradation by the autophagic/lysosomal and proteasomal pathways in atrophying muscle cells
    • Zhao, J., Brault, J.J., Schild, A., Cao, P., Sandri, M., Schiaffino, S., Lecker, S.H. and Goldberg, A.L. (2007) FoxO3 coordinately activates protein degradation by the autophagic/lysosomal and proteasomal pathways in atrophying muscle cells. Cell Metab., 6, 472-483.
    • (2007) Cell Metab. , vol.6 , pp. 472-483
    • Zhao, J.1    Brault, J.J.2    Schild, A.3    Cao, P.4    Sandri, M.5    Schiaffino, S.6    Lecker, S.H.7    Goldberg, A.L.8
  • 23
    • 26444610334 scopus 로고    scopus 로고
    • Calpain 3 participates in sarcomere remodeling by acting upstream of the ubiquitin-proteasome pathway
    • Kramerova, I., Kudryashova, E., Venkatraman, G. and Spencer, M.J. (2005) Calpain 3 participates in sarcomere remodeling by acting upstream of the ubiquitin-proteasome pathway. Hum. Mol. Genet., 14, 2125-2134.
    • (2005) Hum. Mol. Genet. , vol.14 , pp. 2125-2134
    • Kramerova, I.1    Kudryashova, E.2    Venkatraman, G.3    Spencer, M.J.4
  • 24
    • 85047693596 scopus 로고    scopus 로고
    • Activation of caspase-3 is an initial step triggering accelerated muscle proteolysis in catabolic conditions
    • Du, J., Wang, X., Miereles, C., Bailey, J.L., Debigare, R., Zheng, B., Price, S.R. and Mitch, W.E. (2004) Activation of caspase-3 is an initial step triggering accelerated muscle proteolysis in catabolic conditions. J. Clin. Invest., 113, 115-123.
    • (2004) J. Clin. Invest. , vol.113 , pp. 115-123
    • Du, J.1    Wang, X.2    Miereles, C.3    Bailey, J.L.4    Debigare, R.5    Zheng, B.6    Price, S.R.7    Mitch, W.E.8
  • 25
    • 1642366780 scopus 로고    scopus 로고
    • Membrane traffic in skeletal muscle
    • Towler, M.C., Kaufman, S.J. and Brodsky, F.M. (2004) Membrane traffic in skeletal muscle. Traffic, 5, 129-139.
    • (2004) Traffic , vol.5 , pp. 129-139
    • Towler, M.C.1    Kaufman, S.J.2    Brodsky, F.M.3
  • 26
    • 11244278743 scopus 로고    scopus 로고
    • Reorganization of microtubule nucleation during muscle differentiation
    • Bugnard, E., Zaal, K.J. and Ralston, E. (2005) Reorganization of microtubule nucleation during muscle differentiation. Cell Motil. Cytoskeleton, 60, 1-13.
    • (2005) Cell Motil. Cytoskeleton , vol.60 , pp. 1-13
    • Bugnard, E.1    Zaal, K.J.2    Ralston, E.3
  • 27
    • 0021991238 scopus 로고
    • Fate of microtubule-organizing centers during myogenesis in vitro
    • Tassin, A.M., Maro, B. and Bornens, M. (1985) Fate of microtubule-organizing centers during myogenesis in vitro. J. Cell Biol., 100, 35-46.
    • (1985) J. Cell Biol. , vol.100 , pp. 35-46
    • Tassin, A.M.1    Maro, B.2    Bornens, M.3
  • 28
    • 77954906120 scopus 로고    scopus 로고
    • Dynamin 2mutants linked to centronuclearmyopathies form abnormally stable polymers
    • Wang, L., Barylko, B., Byers, C., Ross, J.A., Jameson, D.M. and Albanesi, J.P. (2010) Dynamin 2mutants linked to centronuclearmyopathies form abnormally stable polymers. J. Biol. Chem., 285, 22753-22757.
    • (2010) J. Biol. Chem. , vol.285 , pp. 22753-22757
    • Wang, L.1    Barylko, B.2    Byers, C.3    Ross, J.A.4    Jameson, D.M.5    Albanesi, J.P.6
  • 30
    • 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
  • 31
    • 46249127073 scopus 로고    scopus 로고
    • AAV-mediated intramuscular delivery of myotubularin corrects the myotubular myopathy phenotype in targeted murine muscle and suggests a function in plasma membrane homeostasis
    • Buj-Bello, A., Fougerousse, F., Schwab, Y., Messaddeq, N., Spehner, D., Pierson, C.R., Durand, M., Kretz, C., Danos, O. and Douar, A.M. et al. (2008) AAV-mediated intramuscular delivery of myotubularin corrects the myotubular myopathy phenotype in targeted murine muscle and suggests a function in plasma membrane homeostasis. Hum. Mol. Genet., 17, 2132-2143.
    • (2008) Hum. Mol. Genet. , vol.17 , pp. 2132-2143
    • Buj-Bello, A.1    Fougerousse, F.2    Schwab, Y.3    Messaddeq, N.4    Spehner, D.5    Pierson, C.R.6    Durand, M.7    Kretz, C.8    Danos, O.9    Douar, A.M.10
  • 32
    • 61449203897 scopus 로고    scopus 로고
    • Loss of myotubularin function results in T-tubule disorganization in zebrafish and human myotubular myopathy
    • Dowling, J.J., Vreede, A.P., Low, S.E., Gibbs, E.M., Kuwada, J.Y., Bonnemann, C.G. and Feldman, E.L. (2009) Loss of myotubularin function results in T-tubule disorganization in zebrafish and human myotubular myopathy. PLoS Genet., 5, e1000372.
    • (2009) PLoS Genet. , vol.5
    • Dowling, J.J.1    Vreede, A.P.2    Low, S.E.3    Gibbs, E.M.4    Kuwada, J.Y.5    Bonnemann, C.G.6    Feldman, E.L.7
  • 34
    • 34250838745 scopus 로고    scopus 로고
    • Dysferlin in membrane trafficking and patch repair
    • Glover, L. and Brown, R.H. (2007) Dysferlin in membrane trafficking and patch repair. Traffic, 8, 785-794.
    • (2007) Traffic , vol.8 , pp. 785-794
    • Glover, L.1    Brown, R.H.2
  • 39
    • 33746918740 scopus 로고    scopus 로고
    • Physiological roles of clathrin adaptor AP complexes: lessons from mutant animals
    • Ohno, H. (2006) Physiological roles of clathrin adaptor AP complexes: lessons from mutant animals. J. Biochem., 139, 943-948.
    • (2006) J. Biochem. , vol.139 , pp. 943-948
    • Ohno, H.1
  • 41
    • 58249115047 scopus 로고    scopus 로고
    • Interpreting neonatal lethal phenotypes in mouse mutants: insights into gene function and human diseases
    • Turgeon, B. and Meloche, S. (2009) Interpreting neonatal lethal phenotypes in mouse mutants: insights into gene function and human diseases. Physiol. Rev., 89, 1-26.
    • (2009) Physiol. Rev. , vol.89 , pp. 1-26
    • Turgeon, B.1    Meloche, S.2
  • 43
    • 5144232790 scopus 로고    scopus 로고
    • The alteration of calcium homeostasis in adult dystrophic mdx muscle fibers is worsened by a chronic exercise in vivo
    • doi:10.1016/j.nbd. 2004.06.002
    • Fraysse, B., Liantonio, A., Cetrone, M., Burdi, R., Pierno, S., Frigeri, A., Pisoni, M., Camerino, C. and De Luca, A. (2004) The alteration of calcium homeostasis in adult dystrophic mdx muscle fibers is worsened by a chronic exercise in vivo. Neurobiol. Dis., 17, 144-154. doi:10.1016/j.nbd.2004.06.002
    • (2004) Neurobiol. Dis. , vol.17 , pp. 144-154
    • Fraysse, B.1    Liantonio, A.2    Cetrone, M.3    Burdi, R.4    Pierno, S.5    Frigeri, A.6    Pisoni, M.7    Camerino, C.8    De Luca, A.9
  • 45
    • 77953586729 scopus 로고    scopus 로고
    • Molecular and phenotypic characterization of a mouse model of oculopharyngeal muscular dystrophy reveals severe muscular atrophy restricted to fast glycolytic fibres
    • Trollet, C., Anvar, S.Y., Venema, A., Hargreaves, I.P., Foster, K., Vignaud, A., Ferry, A., Negroni, E., Hourde, C. and Baraibar, M.A. et al. (2010) Molecular and phenotypic characterization of a mouse model of oculopharyngeal muscular dystrophy reveals severe muscular atrophy restricted to fast glycolytic fibres. Hum. Mol. Genet., 19, 2191-2207.
    • (2010) Hum. Mol. Genet. , vol.19 , pp. 2191-2207
    • Trollet, C.1    Anvar, S.Y.2    Venema, A.3    Hargreaves, I.P.4    Foster, K.5    Vignaud, A.6    Ferry, A.7    Negroni, E.8    Hourde, C.9    Baraibar, M.A.10


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.