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Volumn 14, Issue 1, 2012, Pages 35-45

Muscle-Specific RING Finger (MuRF) cDNAs in Atlantic Salmon (Salmo salar) and Their Role as Regulators of Muscle Protein Degradation

Author keywords

Atlantic salmon; E3 ubiquitin ligase; MuRF1; MuRF2; Proteasome; Protein degradation

Indexed keywords

ATLANTIC SALMON; MURF1; MURF2; PROTEASOMES; PROTEIN DEGRADATION; UBIQUITIN LIGASES;

EID: 84855352391     PISSN: 14362228     EISSN: None     Source Type: Journal    
DOI: 10.1007/s10126-011-9385-4     Document Type: Article
Times cited : (20)

References (59)
  • 2
    • 49949152254 scopus 로고    scopus 로고
    • Apoptosis signalling is essential and precedes protein degradation in wasting skeletal muscle during catabolic conditions
    • Argiles JA, Lopez-Soriano FJ, Busquets S (2008) Apoptosis signalling is essential and precedes protein degradation in wasting skeletal muscle during catabolic conditions. Int J Biochem Cell Biol 40: 1674-1678.
    • (2008) Int J Biochem Cell Biol , vol.40 , pp. 1674-1678
    • Argiles, J.A.1    Lopez-Soriano, F.J.2    Busquets, S.3
  • 3
    • 77951464177 scopus 로고    scopus 로고
    • MAFbx/atrogin-1 expression is a poor index of muscle proteolysis
    • Attaix D, Baracos VE (2010) MAFbx/atrogin-1 expression is a poor index of muscle proteolysis. Curr Opin Clin Nutr Metab Care 13: 223-224.
    • (2010) Curr Opin Clin Nutr Metab Care , vol.13 , pp. 223-224
    • Attaix, D.1    Baracos, V.E.2
  • 5
    • 23944525331 scopus 로고    scopus 로고
    • Altered responses in skeletal muscle protein turnover during aging in anabolic and catabolic periods
    • Attaix D, Mosoni L, Dardevet D, Combaret L, Mirand PP, Grizard J (2005) Altered responses in skeletal muscle protein turnover during aging in anabolic and catabolic periods. Int J Biochem Cell Biol 37: 1962-1973.
    • (2005) Int J Biochem Cell Biol , vol.37 , pp. 1962-1973
    • Attaix, D.1    Mosoni, L.2    Dardevet, D.3    Combaret, L.4    Mirand, P.P.5    Grizard, J.6
  • 6
  • 8
    • 33748373603 scopus 로고    scopus 로고
    • Atrophy and hypertrophy of skeletal muscles: structural and functional aspects
    • Boonyarom O, Inui K (2006) Atrophy and hypertrophy of skeletal muscles: structural and functional aspects. Acta Physiol 188: 77-89.
    • (2006) Acta Physiol , vol.188 , pp. 77-89
    • Boonyarom, O.1    Inui, K.2
  • 9
    • 0029977716 scopus 로고    scopus 로고
    • The RING finger domain: a recent example of a sequence-structure family
    • Borden KLB, Freemont PS (1996) The RING finger domain: a recent example of a sequence-structure family. Curr Opin Struct Biol 6: 395-401.
    • (1996) Curr Opin Struct Biol , vol.6 , pp. 395-401
    • Borden, K.L.B.1    Freemont, P.S.2
  • 10
    • 69849087745 scopus 로고    scopus 로고
    • Selection of reference genes for expression studies with fish myogenic cell cultures
    • Bower NI, Johnston IA (2009) Selection of reference genes for expression studies with fish myogenic cell cultures. BMC Molecular Biology 10.
    • (2009) BMC Molecular Biology , vol.10
    • Bower, N.I.1    Johnston, I.A.2
  • 11
    • 69949106349 scopus 로고    scopus 로고
    • Phasing of muscle gene expression with fasting-induced recovery growth in Atlantic salmon
    • Bower NI, Taylor RG, Johnston IA (2009) Phasing of muscle gene expression with fasting-induced recovery growth in Atlantic salmon. Frontiers in Zoology 6.
    • (2009) Frontiers in Zoology , vol.6
    • Bower, N.I.1    Taylor, R.G.2    Johnston, I.A.3
  • 12
    • 77952741030 scopus 로고    scopus 로고
    • Characterisation and differential regulation of MAFbx/Atrogin-1 alpha and beta transcripts in skeletal muscle of Atlantic salmon (Salmo salar)
    • Bower NI, de la Serrana DG, Johnston IA (2010) Characterisation and differential regulation of MAFbx/Atrogin-1 alpha and beta transcripts in skeletal muscle of Atlantic salmon (Salmo salar). Biochem Biophys Res Commun 396: 265-271.
    • (2010) Biochem Biophys Res Commun , vol.396 , pp. 265-271
    • Bower, N.I.1    de la Serrana, D.G.2    Johnston, I.A.3
  • 13
    • 0347823003 scopus 로고    scopus 로고
    • MatGAT: an application that generates similarity/identity matrices using protein or DNA sequences
    • Campanella JJ, Bitincka L, Smalley J (2003) MatGAT: an application that generates similarity/identity matrices using protein or DNA sequences. BMC Bioinformatics 4.
    • (2003) BMC Bioinformatics , vol.4
    • Campanella, J.J.1    Bitincka, L.2    Smalley, J.3
  • 14
    • 4444318673 scopus 로고    scopus 로고
    • The SCF ubiquitin ligase: insights into a molecular machine
    • Cardozo T, Pagano M (2004) The SCF ubiquitin ligase: insights into a molecular machine. Nat Rev Mol Cell Biol 5: 739-751.
    • (2004) Nat Rev Mol Cell Biol , vol.5 , pp. 739-751
    • Cardozo, T.1    Pagano, M.2
  • 18
    • 0028018268 scopus 로고
    • The ubiquitin-proteasome proteolytic pathway
    • Ciechanover A (1994) The ubiquitin-proteasome proteolytic pathway. Cell 79: 13-21.
    • (1994) Cell , vol.79 , pp. 13-21
    • Ciechanover, A.1
  • 19
    • 77956185742 scopus 로고    scopus 로고
    • Molecular characterization of atrogin-1/F-box protein-32 (FBXO32) and F-box protein-25 (FBXO25) in rainbow trout (Oncorhynchus mykiss): Expression across tissues in response to feed deprivation
    • Cleveland BM, Evenhuis JP (2010) Molecular characterization of atrogin-1/F-box protein-32 (FBXO32) and F-box protein-25 (FBXO25) in rainbow trout (Oncorhynchus mykiss): Expression across tissues in response to feed deprivation. Comp Biochem Physiol B Biochem Mol Biol 157: 248-257.
    • (2010) Comp Biochem Physiol B Biochem Mol Biol , vol.157 , pp. 248-257
    • Cleveland, B.M.1    Evenhuis, J.P.2
  • 20
    • 70449640273 scopus 로고    scopus 로고
    • Insulin-like growth factor-I and genetic effects on indexes of protein degradation in response to feed deprivation in rainbow trout (Oncorhynchus mykiss)
    • Cleveland BM, Weber GM, Blemings KP, Silverstein JT (2009) Insulin-like growth factor-I and genetic effects on indexes of protein degradation in response to feed deprivation in rainbow trout (Oncorhynchus mykiss). Am J Physiol Regul Integr Comp Physiol 297: R1332-R1342.
    • (2009) Am J Physiol Regul Integr Comp Physiol , vol.297
    • Cleveland, B.M.1    Weber, G.M.2    Blemings, K.P.3    Silverstein, J.T.4
  • 21
    • 0029979369 scopus 로고    scopus 로고
    • Biologic basis for interleukin-1 in disease
    • Dinarello CA (1996) Biologic basis for interleukin-1 in disease. Blood 87: 2095-2147.
    • (1996) Blood , vol.87 , pp. 2095-2147
    • Dinarello, C.A.1
  • 22
    • 0347915534 scopus 로고    scopus 로고
    • Protein growth rate in rainbow trout (Oncorhynchus mykiss) is negatively correlated to liver 20S proteasome activity
    • Dobly A, Martin SAM, Blaney SC, Houlihan DF (2004) Protein growth rate in rainbow trout (Oncorhynchus mykiss) is negatively correlated to liver 20S proteasome activity. Comp Biochem Physiol A Mol Integr Physiol 137: 75-85.
    • (2004) Comp Biochem Physiol A Mol Integr Physiol , vol.137 , pp. 75-85
    • Dobly, A.1    Martin, S.A.M.2    Blaney, S.C.3    Houlihan, D.F.4
  • 26
    • 0033961923 scopus 로고    scopus 로고
    • Ubiquitination: RING for destruction?
    • Freemont PS (2000) Ubiquitination: RING for destruction? Curr Biol 10: R84-R87.
    • (2000) Curr Biol , vol.10
    • Freemont, P.S.1
  • 27
    • 0041424822 scopus 로고    scopus 로고
    • Molecular mechanisms modulating muscle mass
    • Glass DJ (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
  • 28
    • 0029071646 scopus 로고
    • Functions of the proteasome-the lysis at the end of the tunnel
    • Goldberg AL (1995) Functions of the proteasome-the lysis at the end of the tunnel. Science 268: 522-523.
    • (1995) Science , vol.268 , pp. 522-523
    • Goldberg, A.L.1
  • 30
    • 33645134674 scopus 로고    scopus 로고
    • Starvation induced alterations in hepatic lysine metabolism in different families of rainbow trout (Oncorhynchus mykiss)
    • Higgins AD, Silverstein JT, Engles J, Wilson ME, Rexroad CE, Blemings KP (2005) Starvation induced alterations in hepatic lysine metabolism in different families of rainbow trout (Oncorhynchus mykiss). Fish Physiol Biochem 31: 33-44.
    • (2005) Fish Physiol Biochem , vol.31 , pp. 33-44
    • Higgins, A.D.1    Silverstein, J.T.2    Engles, J.3    Wilson, M.E.4    Rexroad, C.E.5    Blemings, K.P.6
  • 32
    • 0036282703 scopus 로고    scopus 로고
    • The SCF ubiquitin ligase: an extended look
    • Jackson PK, Eldridge AG (2002) The SCF ubiquitin ligase: an extended look. Mol Cell 9: 923-925.
    • (2002) Mol Cell , vol.9 , pp. 923-925
    • Jackson, P.K.1    Eldridge, A.G.2
  • 33
    • 11144237310 scopus 로고    scopus 로고
    • Muscle-specific RING finger 1 is a bona fide ubiquitin ligase that degrades cardiac troponin I
    • Kedar V, McDonough H, Arya R, Li HH, Rockman HA, Patterson C (2004) Muscle-specific RING finger 1 is a bona fide ubiquitin ligase that degrades cardiac troponin I. Proc Natl Acad Sci USA 101: 18135-18140.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 18135-18140
    • Kedar, V.1    McDonough, H.2    Arya, R.3    Li, H.H.4    Rockman, H.A.5    Patterson, C.6
  • 34
    • 0033989986 scopus 로고    scopus 로고
    • Modes of regulation of ubiquitin-mediated protein degradation
    • Kornitzer D, Ciechanover A (2000) Modes of regulation of ubiquitin-mediated protein degradation. J Cell Physiol 182: 1-11.
    • (2000) J Cell Physiol , vol.182 , pp. 1-11
    • Kornitzer, D.1    Ciechanover, A.2
  • 35
    • 3242810318 scopus 로고    scopus 로고
    • MEGA3: integrated software for molecular evolutionary genetics analysis and sequence alignment
    • Kumar S, Tamura K, Nei M (2004) MEGA3: integrated software for molecular evolutionary genetics analysis and sequence alignment. Brief Bioinform 5: 150-163.
    • (2004) Brief Bioinform , vol.5 , pp. 150-163
    • Kumar, S.1    Tamura, K.2    Nei, M.3
  • 36
    • 12244252222 scopus 로고    scopus 로고
    • Slowing muscle atrophy: putting the brakes on protein breakdown
    • Lecker SH, Goldberg AL (2002) Slowing muscle atrophy: putting the brakes on protein breakdown. J Physiol Lond 545: 729.
    • (2002) J Physiol Lond , vol.545 , pp. 729
    • Lecker, S.H.1    Goldberg, A.L.2
  • 38
    • 9644270401 scopus 로고    scopus 로고
    • Atrogin-1/rnuscle atrophy F-box inhibits calcineurin-dependent cardiac hypertrophy by participating in an SCF ubiquitin ligase complex
    • Li HH, Kedar V, Zhang CL, McDonough H, Arya R, Wang DZ, Patterson C (2004) Atrogin-1/rnuscle atrophy F-box inhibits calcineurin-dependent cardiac hypertrophy by participating in an SCF ubiquitin ligase complex. J Clin Investig 114: 1058-1071.
    • (2004) J Clin Investig , vol.114 , pp. 1058-1071
    • Li, H.H.1    Kedar, V.2    Zhang, C.L.3    McDonough, H.4    Arya, R.5    Wang, D.Z.6    Patterson, C.7
  • 40
    • 0036451733 scopus 로고    scopus 로고
    • Ubiquitin-proteasome-dependent proteolysis in rainbow trout (Oncorhynchus mykiss): effect of food deprivation
    • Martin SAM, Blaney S, Bowman AS, Houlihan DF (2002) Ubiquitin-proteasome-dependent proteolysis in rainbow trout (Oncorhynchus mykiss): effect of food deprivation. Pflügers Arch Eur J Physiol 445: 257-266.
    • (2002) Pflügers Arch Eur J Physiol , vol.445 , pp. 257-266
    • Martin, S.A.M.1    Blaney, S.2    Bowman, A.S.3    Houlihan, D.F.4
  • 41
    • 77954169879 scopus 로고    scopus 로고
    • Starvation alters the liver transcriptome of the innate immune response in Atlantic salmon (Salmo salar)
    • Martin SAM, Douglas A, Houlihan DF, Secombes CJ (2010) Starvation alters the liver transcriptome of the innate immune response in Atlantic salmon (Salmo salar). BMC Genomics 11: 418.
    • (2010) BMC Genomics , vol.11 , pp. 418
    • Martin, S.A.M.1    Douglas, A.2    Houlihan, D.F.3    Secombes, C.J.4
  • 42
    • 4344598187 scopus 로고    scopus 로고
    • Muscle-specific RING finger-2 (MURF-2) is important for microtubule, intermediate filament and sarcomeric M-line maintenance in striated muscle development
    • McElhinny AS, Perry CN, Witt CC, Labeit S, Gregorio CC (2004) Muscle-specific RING finger-2 (MURF-2) is important for microtubule, intermediate filament and sarcomeric M-line maintenance in striated muscle development. J Cell Sci 117: 3175-3188.
    • (2004) J Cell Sci , vol.117 , pp. 3175-3188
    • McElhinny, A.S.1    Perry, C.N.2    Witt, C.C.3    Labeit, S.4    Gregorio, C.C.5
  • 43
    • 30444452500 scopus 로고    scopus 로고
    • TRIM/RBCC, a novel class of 'single protein RING finger' E3 ubiquitin ligases
    • Meroni G, Diez-Roux G (2005) TRIM/RBCC, a novel class of 'single protein RING finger' E3 ubiquitin ligases. BioEssays 27: 1147-1157.
    • (2005) BioEssays , vol.27 , pp. 1147-1157
    • Meroni, G.1    Diez-Roux, G.2
  • 46
    • 0033386408 scopus 로고    scopus 로고
    • Selective changes in the protein-turnover rates and nature of growth induced in trout liver by long-term starvation followed by re-feeding
    • Peragon J, Barroso JB, Garcia-Salguero L, Aranda F, de la Higuera M, Lupianez JA (1999) Selective changes in the protein-turnover rates and nature of growth induced in trout liver by long-term starvation followed by re-feeding. Mol Cell Biochem 201: 1-10.
    • (1999) Mol Cell Biochem , vol.201 , pp. 1-10
    • Peragon, J.1    Barroso, J.B.2    Garcia-Salguero, L.3    Aranda, F.4    de la Higuera, M.5    Lupianez, J.A.6
  • 47
    • 17344392308 scopus 로고    scopus 로고
    • A new mathematical model for relative quantification in real-time RT-PCR
    • Pfaffl MW (2001) A new mathematical model for relative quantification in real-time RT-PCR. Nucleic Acids Research 29.
    • (2001) Nucleic Acids Research , vol.29
    • Pfaffl, M.W.1
  • 48
    • 0034915764 scopus 로고    scopus 로고
    • Mechanisms underlying ubiquitination
    • Pickart CM (2001) Mechanisms underlying ubiquitination. Annu Rev Biochem 70: 503-533.
    • (2001) Annu Rev Biochem , vol.70 , pp. 503-533
    • Pickart, C.M.1
  • 49
    • 33846015010 scopus 로고    scopus 로고
    • Rapid disuse and denervation atrophy involve transcriptional changes similar to those of muscle wasting during systemic diseases
    • Sacheck JM, Hyatt JPK, Raffaello A, Jagoe RT, Roy RR, Edgerton VR, Lecker SH, Goldberg AL (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.K.2    Raffaello, A.3    Jagoe, R.T.4    Roy, R.R.5    Edgerton, V.R.6    Lecker, S.H.7    Goldberg, A.L.8
  • 50
    • 33646364780 scopus 로고    scopus 로고
    • Molecular characterization of muscle atrophy and proteolysis associated with spawning in rainbow trout
    • Salem M, Kenney PB, Rexroad CE, Yao JB (2006) Molecular characterization of muscle atrophy and proteolysis associated with spawning in rainbow trout. Comp Biochem Physiol, D: Genomics Proteomics 1: 227-237.
    • (2006) Comp Biochem Physiol, D: Genomics Proteomics , vol.1 , pp. 227-237
    • Salem, M.1    Kenney, P.B.2    Rexroad, C.E.3    Yao, J.B.4
  • 51
    • 40449090579 scopus 로고    scopus 로고
    • Feeding status regulates the polyubiquitination step of the ubiquitin-proteasome-dependent proteolysis in rainbow trout (Oncorhynchus mykiss) muscle
    • Seiliez I, Panserat S, Skiba-Cassy S, Fricot A, Vachot C, Kaushik S, Tesseraud S (2008) Feeding status regulates the polyubiquitination step of the ubiquitin-proteasome-dependent proteolysis in rainbow trout (Oncorhynchus mykiss) muscle. J Nutr 138: 487-491.
    • (2008) J Nutr , vol.138 , pp. 487-491
    • Seiliez, I.1    Panserat, S.2    Skiba-Cassy, S.3    Fricot, A.4    Vachot, C.5    Kaushik, S.6    Tesseraud, S.7
  • 53
    • 0034698695 scopus 로고    scopus 로고
    • Regulation of microtubule dynamics and myogenic differentiation by MURF, a striated muscle RING-finger protein
    • Spencer JA, Eliazer S, Ilaria RL, Richardson JA, Olson EN (2000) Regulation of microtubule dynamics and myogenic differentiation by MURF, a striated muscle RING-finger protein. J Cell Biol 150: 771-784.
    • (2000) J Cell Biol , vol.150 , pp. 771-784
    • Spencer, J.A.1    Eliazer, S.2    Ilaria, R.L.3    Richardson, J.A.4    Olson, E.N.5
  • 56
    • 0032867676 scopus 로고    scopus 로고
    • The 26S proteasome: a molecular machine designed for controlled proteolysis
    • Voges D, Zwickl P, Baumeister W (1999) The 26S proteasome: a molecular machine designed for controlled proteolysis. Annu Rev Biochem 68: 1015-1068.
    • (1999) Annu Rev Biochem , vol.68 , pp. 1015-1068
    • Voges, D.1    Zwickl, P.2    Baumeister, W.3
  • 57
    • 15544377813 scopus 로고    scopus 로고
    • Genome evolution and biodiversity in teleost fish
    • Volff JN (2005) Genome evolution and biodiversity in teleost fish. Heredity 94: 280-294.
    • (2005) Heredity , vol.94 , pp. 280-294
    • Volff, J.N.1
  • 58
    • 38549139612 scopus 로고    scopus 로고
    • Cooperative control of striated muscle mass and metabolism by MuRF1 and MuRF2
    • Witt CC, Witt SH, Lerche S, Labeit D, Back W, Labeit S (2008) Cooperative control of striated muscle mass and metabolism by MuRF1 and MuRF2. EMBO J 27: 350-360.
    • (2008) EMBO J , vol.27 , pp. 350-360
    • Witt, C.C.1    Witt, S.H.2    Lerche, S.3    Labeit, D.4    Back, W.5    Labeit, S.6
  • 59
    • 3042569682 scopus 로고    scopus 로고
    • Dogmas and controversies in the handling of nitrogenous wastes: expression of arginase Type I and II genes in rainbow trout: influence of fasting on liver enzyme activity and mRNA levels in juveniles
    • Wright PA, Campbell A, Morgan RL, Rosenberger AG, Murray BW (2004) Dogmas and controversies in the handling of nitrogenous wastes: expression of arginase Type I and II genes in rainbow trout: influence of fasting on liver enzyme activity and mRNA levels in juveniles. J Exp Biol 207: 2033-2042.
    • (2004) J Exp Biol , vol.207 , pp. 2033-2042
    • Wright, P.A.1    Campbell, A.2    Morgan, R.L.3    Rosenberger, A.G.4    Murray, B.W.5


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