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Volumn 22, Issue 24, 2013, Pages 4967-4977

MYBPC1 mutations impair skeletal muscle function in zebrafish models of arthrogryposis

Author keywords

[No Author keywords available]

Indexed keywords

MESSENGER RNA;

EID: 84888150799     PISSN: 09646906     EISSN: 14602083     Source Type: Journal    
DOI: 10.1093/hmg/ddt344     Document Type: Article
Times cited : (48)

References (49)
  • 2
    • 0021948713 scopus 로고
    • Genetic aspects of arthrogryposis
    • Hall, J.G. (1985) Genetic aspects of arthrogryposis. Clin. Ortho. Relat. Res., 194, 44-53.
    • (1985) Clin. Ortho. Relat. Res. , vol.194 , pp. 44-53
    • Hall, J.G.1
  • 3
    • 33646364575 scopus 로고    scopus 로고
    • Mutations in embryonic myosin heavy chain(MYH3) cause Freeman-Sheldon syndromeand Sheldon-Hall syndrome
    • Toydemir, R.M., Rutherford, A., Whitby, F.G., Jorde, L.B., Carey, J.C. and Bamshad, M.J. (2006) Mutations in embryonic myosin heavy chain(MYH3) cause Freeman-Sheldon syndromeand Sheldon-Hall syndrome. Nat. Genet., 38, 561-565.
    • (2006) Nat. Genet. , vol.38 , pp. 561-565
    • Toydemir, R.M.1    Rutherford, A.2    Whitby, F.G.3    Jorde, L.B.4    Carey, J.C.5    Bamshad, M.J.6
  • 4
    • 33947541830 scopus 로고    scopus 로고
    • Distal arthrogryposis and muscle weakness associated with a beta-tropomyosin mutation
    • Tajsharghi, H., Kimber, E., Holmgren, D., Tulinius, M. and Oldfors, A. (2007) Distal arthrogryposis and muscle weakness associated with a beta-tropomyosin mutation. Neurology, 68, 772-775.
    • (2007) Neurology , vol.68 , pp. 772-775
    • Tajsharghi, H.1    Kimber, E.2    Holmgren, D.3    Tulinius, M.4    Oldfors, A.5
  • 6
    • 0038389782 scopus 로고    scopus 로고
    • Mutations in TNNT3 cause multiple congenital contractures: a second locus for distal arthrogryposis type 2B
    • Sung, S.S., Brassington, A.M., Krakowiak, P.A., Carey, J.C., Jorde, L.B. and Bamshad, M. (2003) Mutations in TNNT3 cause multiple congenital contractures: a second locus for distal arthrogryposis type 2B. Am. J. Hum. Genet., 73, 212-214.
    • (2003) Am. J. Hum. Genet. , vol.73 , pp. 212-214
    • Sung, S.S.1    Brassington, A.M.2    Krakowiak, P.A.3    Carey, J.C.4    Jorde, L.B.5    Bamshad, M.6
  • 9
    • 0015924821 scopus 로고
    • A new protein of the thick filaments of vertebrate skeletal myofibrils. Extractions, purification and characterization
    • Offer, G., Moos, C. and Starr, R. (1973)A new protein of the thick filaments of vertebrate skeletal myofibrils. Extractions, purification and characterization. J. Mol. Biol., 74, 653-676.
    • (1973) J. Mol. Biol. , vol.74 , pp. 653-676
    • Offer, G.1    Moos, C.2    Starr, R.3
  • 10
    • 0029029027 scopus 로고
    • Phosphorylation switches specific for the cardiac isoform of myosin binding protein-C: a modulator of cardiac contraction?
    • Gautel, M., Zuffardi, O., Freiburg, A. and Labeit, S. (1995) Phosphorylation switches specific for the cardiac isoform of myosin binding protein-C: a modulator of cardiac contraction? EMBO J., 14, 1952-1960.
    • (1995) EMBO J. , vol.14 , pp. 1952-1960
    • Gautel, M.1    Zuffardi, O.2    Freiburg, A.3    Labeit, S.4
  • 11
    • 0027168759 scopus 로고
    • Differential expression, conserved domain structure and chromosome assignment
    • Weber, F.E., Vaughan, K.T., Reinach, F.C. and Fischman, D.A. (1993) Complete sequence of human fast-type and slow-type muscle myosin-binding-protein C (MyBP-C). Differential expression, conserved domain structure and chromosome assignment. Eur. J. Biochem., 216, 661-669.
    • (1993) Eur. J. Biochem. , vol.216 , pp. 661-669
    • Weber, F.E.1    Vaughan, K.T.2    Reinach, F.C.3    Fischman, D.A.4
  • 14
    • 84866299419 scopus 로고    scopus 로고
    • Autosomal recessive lethal congenital contractural syndrome type 4 (LCCS4) caused by a mutation in MYBPC1
    • Markus, B., Narkis, G., Landau, D., Birk, R.Z., Cohen, I. and Birk, O.S. (2012) Autosomal recessive lethal congenital contractural syndrome type 4 (LCCS4) caused by a mutation in MYBPC1. Hum. Mut., 33, 1435-1438.
    • (2012) Hum. Mut. , vol.33 , pp. 1435-1438
    • Markus, B.1    Narkis, G.2    Landau, D.3    Birk, R.Z.4    Cohen, I.5    Birk, O.S.6
  • 15
    • 79953184636 scopus 로고    scopus 로고
    • Signaling and myosin-binding protein C
    • James, J. and Robbins, J. (2011) Signaling and myosin-binding protein C. J. Biol. Chem., 286, 9913-9919.
    • (2011) J. Biol. Chem. , vol.286 , pp. 9913-9919
    • James, J.1    Robbins, J.2
  • 16
    • 0027515217 scopus 로고
    • The major myosin-binding domain of skeletal muscle MyBP-C (C protein) resides in the COOH-terminal, immunoglobulin C2 motif
    • Okagaki, T., Weber, F.E., Fischman, D.A., Vaughan, K.T., Mikawa, T. and Reinach, F.C. (1993) The major myosin-binding domain of skeletal muscle MyBP-C (C protein) resides in the COOH-terminal, immunoglobulin C2 motif. J. Cell Biol., 123, 619-626.
    • (1993) J. Cell Biol. , vol.123 , pp. 619-626
    • Okagaki, T.1    Weber, F.E.2    Fischman, D.A.3    Vaughan, K.T.4    Mikawa, T.5    Reinach, F.C.6
  • 17
    • 0030052266 scopus 로고    scopus 로고
    • A molecular map of the interactions between titin and myosin-binding protein C. Implications for sarcomeric assembly in familial hypertrophic cardiomyopathy
    • Freiburg, A. and Gautel, M. (1996) A molecular map of the interactions between titin and myosin-binding protein C. Implications for sarcomeric assembly in familial hypertrophic cardiomyopathy. Eur. J. Biochem., 235, 317-323.
    • (1996) Eur. J. Biochem. , vol.235 , pp. 317-323
    • Freiburg, A.1    Gautel, M.2
  • 18
    • 0033605334 scopus 로고    scopus 로고
    • Mutations in beta-myosin S2 that cause familial hypertrophic cardiomyopathy (FHC) abolish the interaction with the regulatory domain of myosin-binding protein-C
    • Gruen, M. and Gautel, M. (1999) Mutations in beta-myosin S2 that cause familial hypertrophic cardiomyopathy (FHC) abolish the interaction with the regulatory domain of myosin-binding protein-C. J. Mol. Biol., 286, 933-949.
    • (1999) J. Mol. Biol. , vol.286 , pp. 933-949
    • Gruen, M.1    Gautel, M.2
  • 19
    • 0018126953 scopus 로고
    • The binding of skeletal muscle C-protein to F-actin, and its relation to the interaction of actin with myosin subfragment-1
    • Moos, C., Mason, C.M., Besterman, J.M., Feng, I.N. and Dubin, J.H. (1978) The binding of skeletal muscle C-protein to F-actin, and its relation to the interaction of actin with myosin subfragment-1. J. Mol. Biol., 124, 571-586.
    • (1978) J. Mol. Biol. , vol.124 , pp. 571-586
    • Moos, C.1    Mason, C.M.2    Besterman, J.M.3    Feng, I.N.4    Dubin, J.H.5
  • 20
  • 21
    • 80053896195 scopus 로고    scopus 로고
    • Myosin binding protein-C slow is a novel substrate for protein kinaseA(PKA) andC (PKC) in skeletal muscle
    • Ackermann, M.A. and Kontrogianni-Konstantopoulos, A. (2011) Myosin binding protein-C slow is a novel substrate for protein kinaseA(PKA) andC (PKC) in skeletal muscle. J. Proteome Res., 10, 4547-4555.
    • (2011) J. Proteome Res. , vol.10 , pp. 4547-4555
    • Ackermann, M.A.1    Kontrogianni-Konstantopoulos, A.2
  • 22
    • 79956011145 scopus 로고    scopus 로고
    • Slow skeletal muscle myosin-binding protein-C(MyBPC1)mediates recruitment of muscle-type creatine kinase (CK) to myosin
    • Chen, Z., Zhao, T.J., Li, J., Gao, Y.S., Meng, F.G., Yan, Y.B. and Zhou, H.M. (2011) Slow skeletal muscle myosin-binding protein-C(MyBPC1)mediates recruitment of muscle-type creatine kinase (CK) to myosin. Biochem. J., 436, 437-445.
    • (2011) Biochem. J. , vol.436 , pp. 437-445
    • Chen, Z.1    Zhao, T.J.2    Li, J.3    Gao, Y.S.4    Meng, F.G.5    Yan, Y.B.6    Zhou, H.M.7
  • 23
    • 84870950547 scopus 로고    scopus 로고
    • Cardiac myosin binding protein-C restricts intrafilament torsional dynamics of actin in a phosphorylation-dependent manner
    • Colson, B.A., Rybakova, I.N., Prochniewicz, E., Moss, R.L. and Thomas, D.D. (2012) Cardiac myosin binding protein-C restricts intrafilament torsional dynamics of actin in a phosphorylation-dependent manner. Proc. Natl Acad. Sci. USA, 109, 20437-20442.
    • (2012) Proc. Natl Acad. Sci. USA , vol.109 , pp. 20437-20442
    • Colson, B.A.1    Rybakova, I.N.2    Prochniewicz, E.3    Moss, R.L.4    Thomas, D.D.5
  • 24
    • 77951634985 scopus 로고    scopus 로고
    • Phosphorylation and function of cardiac myosin binding protein-C in health and disease
    • Barefield, D. and Sadayappan, S. (2010) Phosphorylation and function of cardiac myosin binding protein-C in health and disease. J. Mol. Cell. Cardiol., 48, 866-875.
    • (2010) J. Mol. Cell. Cardiol. , vol.48 , pp. 866-875
    • Barefield, D.1    Sadayappan, S.2
  • 28
    • 0033774310 scopus 로고    scopus 로고
    • Asynchronous activation of 10 muscle-specific protein (MSP) genes during zebrafish somitogenesis
    • Xu, Y., He, J., Wang, X., Lim, T.M. and Gong, Z. (2000) Asynchronous activation of 10 muscle-specific protein (MSP) genes during zebrafish somitogenesis. Dev. Dyn., 219, 201-215.
    • (2000) Dev. Dyn. , vol.219 , pp. 201-215
    • Xu, Y.1    He, J.2    Wang, X.3    Lim, T.M.4    Gong, Z.5
  • 29
    • 0024311374 scopus 로고
    • Evolutionarily conserved sequences of striated muscle myosin heavy chain isoforms. Epitope mapping by cDNA expression
    • Miller, J.B., Teal, S.B. and Stockdale, F.E. (1989) Evolutionarily conserved sequences of striated muscle myosin heavy chain isoforms. Epitope mapping by cDNA expression. J. Biol. Chem., 264, 13122-13130.
    • (1989) J. Biol. Chem. , vol.264 , pp. 13122-13130
    • Miller, J.B.1    Teal, S.B.2    Stockdale, F.E.3
  • 31
    • 0031768122 scopus 로고    scopus 로고
    • Time course of the development of motor behaviors in the zebrafish embryo
    • Saint-Amant, L. and Drapeau, P. (1998) Time course of the development of motor behaviors in the zebrafish embryo. J. Neurobiol., 37, 622-632.
    • (1998) J. Neurobiol. , vol.37 , pp. 622-632
    • Saint-Amant, L.1    Drapeau, P.2
  • 32
    • 80955180211 scopus 로고    scopus 로고
    • Developmental transition of touch response from slow muscle-mediated coilings to fast muscle-mediated burst swimming in zebrafish
    • Naganawa, Y. and Hirata, H. (2011) Developmental transition of touch response from slow muscle-mediated coilings to fast muscle-mediated burst swimming in zebrafish. Dev. Biol., 355, 194-204.
    • (2011) Dev. Biol. , vol.355 , pp. 194-204
    • Naganawa, Y.1    Hirata, H.2
  • 34
    • 27944447613 scopus 로고    scopus 로고
    • Expression of slow skeletal myosin binding C-protein in normal adult mammalian heart
    • Dhoot, G.K. and Perry, S.V. (2005) Expression of slow skeletal myosin binding C-protein in normal adult mammalian heart. J. Muscle Res. Cell Motil., 26, 143-148.
    • (2005) J. Muscle Res. Cell Motil. , vol.26 , pp. 143-148
    • Dhoot, G.K.1    Perry, S.V.2
  • 35
  • 36
    • 0031055854 scopus 로고    scopus 로고
    • Organization and sequence of human cardiac myosin binding proteinCgene(MYBPC3) and identification of mutations predicted to produce truncated proteins in familial hypertrophic cardiomyopathy
    • Carrier, L., Bonne, G., Bahrend, E., Yu, B., Richard, P., Niel, F., Hainque, B., Cruaud, C., Gary, F., Labeit, S. et al. (1997) Organization and sequence of human cardiac myosin binding proteinCgene(MYBPC3) and identification of mutations predicted to produce truncated proteins in familial hypertrophic cardiomyopathy. Circ. Res., 80, 427-434.
    • (1997) Circ. Res. , vol.80 , pp. 427-434
    • Carrier, L.1    Bonne, G.2    Bahrend, E.3    Yu, B.4    Richard, P.5    Niel, F.6    Hainque, B.7    Cruaud, C.8    Gary, F.9    Labeit, S.10
  • 37
    • 0345131725 scopus 로고    scopus 로고
    • Isoform transitions of the myosin binding protein C family in developing human and mouse muscles: lack of isoform transcomplementation in cardiac muscle
    • Gautel, M., Furst, D.O., Cocco, A. and Schiaffino, S. (1998) Isoform transitions of the myosin binding protein C family in developing human and mouse muscles: lack of isoform transcomplementation in cardiac muscle. Circ. Res., 82, 124-129.
    • (1998) Circ. Res. , vol.82 , pp. 124-129
    • Gautel, M.1    Furst, D.O.2    Cocco, A.3    Schiaffino, S.4
  • 40
    • 84860907995 scopus 로고    scopus 로고
    • Alpha-actinin-2 deficiency results in sarcomeric defects in zebrafish that cannot be rescued by alpha-actinin-3 revealing functional differences between sarcomeric isoforms
    • Gupta, V., Discenza, M., Guyon, J.R., Kunkel, L.M. and Beggs, A.H. (2012) Alpha-actinin-2 deficiency results in sarcomeric defects in zebrafish that cannot be rescued by alpha-actinin-3 revealing functional differences between sarcomeric isoforms. FASEB J., 26, 1892-1908.
    • (2012) FASEB J. , vol.26 , pp. 1892-1908
    • Gupta, V.1    Discenza, M.2    Guyon, J.R.3    Kunkel, L.M.4    Beggs, A.H.5
  • 41
    • 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
  • 42
    • 77649136075 scopus 로고    scopus 로고
    • Loss of Smyhc1 or Hsp90alpha1 function results in different effects on myofibril organization in skeletal muscles of zebrafish embryos
    • Codina, M., Li, J., Gutierrez, J., Kao, J.P. and Du, S.J. (2010) Loss of Smyhc1 or Hsp90alpha1 function results in different effects on myofibril organization in skeletal muscles of zebrafish embryos. PLoSONE, 5, e8416.
    • (2010) PLoSONE , vol.5
    • Codina, M.1    Li, J.2    Gutierrez, J.3    Kao, J.P.4    Du, S.J.5
  • 44
    • 70349994804 scopus 로고    scopus 로고
    • Depletion of zebrafish Tcap leads to muscular dystrophy via disrupting sarcomere-membrane interaction, not sarcomere assembly
    • Zhang, R., Yang, J., Zhu, J. and Xu, X. (2009) Depletion of zebrafish Tcap leads to muscular dystrophy via disrupting sarcomere-membrane interaction, not sarcomere assembly. Hum. Mol. Genet., 18, 4130-4140.
    • (2009) Hum. Mol. Genet. , vol.18 , pp. 4130-4140
    • Zhang, R.1    Yang, J.2    Zhu, J.3    Xu, X.4
  • 46
    • 0033615665 scopus 로고    scopus 로고
    • Limb deformations in oligohydramnios sequence: effects of gestational age and duration of oligohydramnios
    • Christianson, C., Huff, D. and McPherson, E. (1999) Limb deformations in oligohydramnios sequence: effects of gestational age and duration of oligohydramnios. Am. J. Med. Genet. A, 86, 430-433.
    • (1999) Am. J. Med. Genet. A , vol.86 , pp. 430-433
    • Christianson, C.1    Huff, D.2    McPherson, E.3


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