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Volumn 584, Issue 14, 2010, Pages 2974-2980

Are biological sensors modulated by their structural scaffolds? The role of the structural muscle proteins α-actinin-2 and α-actinin-3 as modulators of biological sensors

Author keywords

Actinin; Biological sensor; Skeletal muscle; Structural scaffold

Indexed keywords

ALPHA ACTININ 2; ALPHA ACTININ 3; CALCIUM ION; CALMODULIN; SCAFFOLD PROTEIN; VOLTAGE GATED POTASSIUM CHANNEL; ACTININ; MUSCLE PROTEIN; PROTEIN;

EID: 77954177590     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2010.05.059     Document Type: Review
Times cited : (20)

References (87)
  • 1
    • 3342973781 scopus 로고    scopus 로고
    • A gene for speed? The evolution and function of alpha-actinin-3
    • MacArthur D.G., North K.N. A gene for speed? The evolution and function of alpha-actinin-3. BioEssays 2004, 26:786-795.
    • (2004) BioEssays , vol.26 , pp. 786-795
    • MacArthur, D.G.1    North, K.N.2
  • 2
    • 0026786782 scopus 로고
    • Cloning and characterization of two human skeletal muscle alpha-actinin genes located on chromosomes 1 and 11
    • Beggs A.H., Byers T.J., Knoll J.H., Boyce F.M., Bruns G.A., Kunkel L.M. Cloning and characterization of two human skeletal muscle alpha-actinin genes located on chromosomes 1 and 11. J. Biol. Chem. 1992, 267:9281-9288.
    • (1992) J. Biol. Chem. , vol.267 , pp. 9281-9288
    • Beggs, A.H.1    Byers, T.J.2    Knoll, J.H.3    Boyce, F.M.4    Bruns, G.A.5    Kunkel, L.M.6
  • 3
    • 0035875090 scopus 로고    scopus 로고
    • Differential expression of the actin-binding proteins, alpha-actinin-2 and -3, in different species: implications for the evolution of functional redundancy
    • Mills M., Yang N., Weinberger R., Vander Woude D.L., Beggs A.H., Easteal S., North K. Differential expression of the actin-binding proteins, alpha-actinin-2 and -3, in different species: implications for the evolution of functional redundancy. Hum. Mol. Genet. 2001, 10:1335-1346.
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 1335-1346
    • Mills, M.1    Yang, N.2    Weinberger, R.3    Vander Woude, D.L.4    Beggs, A.H.5    Easteal, S.6    North, K.7
  • 4
    • 34748849262 scopus 로고    scopus 로고
    • Loss of ACTN3 gene function alters mouse muscle metabolism and shows evidence of positive selection in humans
    • MacArthur D.G., et al. Loss of ACTN3 gene function alters mouse muscle metabolism and shows evidence of positive selection in humans. Nat. Genet. 2007, 39:1261-1265.
    • (2007) Nat. Genet. , vol.39 , pp. 1261-1265
    • MacArthur, D.G.1
  • 5
  • 7
    • 21644474657 scopus 로고    scopus 로고
    • ACTN3 genotype is associated with increases in muscle strength in response to resistance training in women
    • Clarkson P.M., et al. ACTN3 genotype is associated with increases in muscle strength in response to resistance training in women. J. Appl. Physiol. 2005, 99:154-163.
    • (2005) J. Appl. Physiol. , vol.99 , pp. 154-163
    • Clarkson, P.M.1
  • 8
    • 33845524821 scopus 로고    scopus 로고
    • Association analysis of the ACTN3 R577X polymorphism and complex quantitative body composition and performance phenotypes in adolescent Greeks
    • Moran C.N., et al. Association analysis of the ACTN3 R577X polymorphism and complex quantitative body composition and performance phenotypes in adolescent Greeks. Eur. J. Hum. Genet. 2007, 15:88-93.
    • (2007) Eur. J. Hum. Genet. , vol.15 , pp. 88-93
    • Moran, C.N.1
  • 9
    • 62649121542 scopus 로고    scopus 로고
    • A genome-wide survey of the prevalence and evolutionary forces acting on human nonsense SNPs
    • Yngvadottir B., et al. A genome-wide survey of the prevalence and evolutionary forces acting on human nonsense SNPs. Am. J. Hum. Genet. 2009, 84:224-234.
    • (2009) Am. J. Hum. Genet. , vol.84 , pp. 224-234
    • Yngvadottir, B.1
  • 10
    • 41849132836 scopus 로고    scopus 로고
    • An Actn3 knockout mouse provides mechanistic insights into the association between alpha-actinin-3 deficiency and human athletic performance
    • MacArthur D.G., et al. An Actn3 knockout mouse provides mechanistic insights into the association between alpha-actinin-3 deficiency and human athletic performance. Hum. Mol. Genet. 2008, 17:1076-1086.
    • (2008) Hum. Mol. Genet. , vol.17 , pp. 1076-1086
    • MacArthur, D.G.1
  • 11
    • 57049097034 scopus 로고    scopus 로고
    • A gene for speed: contractile properties of isolated whole EDL muscle from an alpha-actinin-3 knockout mouse
    • Chan S., Seto J.T., MacArthur D.G., Yang N., North K.N., Head S.I. A gene for speed: contractile properties of isolated whole EDL muscle from an alpha-actinin-3 knockout mouse. Am. J. Physiol. Cell Physiol. 2008, 295:C897-C904.
    • (2008) Am. J. Physiol. Cell Physiol. , vol.295
    • Chan, S.1    Seto, J.T.2    MacArthur, D.G.3    Yang, N.4    North, K.N.5    Head, S.I.6
  • 14
    • 70149085458 scopus 로고    scopus 로고
    • Phosphofructo-1-kinase deficiency leads to a severe cardiac and hematological disorder in addition to skeletal muscle glycogenosis
    • Garcia M., et al. Phosphofructo-1-kinase deficiency leads to a severe cardiac and hematological disorder in addition to skeletal muscle glycogenosis. PLoS Genet. 2009, 5:e1000615.
    • (2009) PLoS Genet. , vol.5
    • Garcia, M.1
  • 15
    • 0029738727 scopus 로고    scopus 로고
    • Disruption of muscle architecture and myocardial degeneration in mice lacking desmin
    • Milner D.J., Weitzer G., Tran D., Bradley A., Capetanaki Y. Disruption of muscle architecture and myocardial degeneration in mice lacking desmin. J. Cell Biol. 1996, 134:1255-1270.
    • (1996) J. Cell Biol. , vol.134 , pp. 1255-1270
    • Milner, D.J.1    Weitzer, G.2    Tran, D.3    Bradley, A.4    Capetanaki, Y.5
  • 16
    • 33845801599 scopus 로고    scopus 로고
    • Targeted deletion of the muscular dystrophy gene myotilin does not perturb muscle structure or function in mice
    • Moza M., Mologni L., Trokovic R., Faulkner G., Partanen J., Carpen O. Targeted deletion of the muscular dystrophy gene myotilin does not perturb muscle structure or function in mice. Mol. Cell Biol. 2007, 27:244-252.
    • (2007) Mol. Cell Biol. , vol.27 , pp. 244-252
    • Moza, M.1    Mologni, L.2    Trokovic, R.3    Faulkner, G.4    Partanen, J.5    Carpen, O.6
  • 18
    • 0030729730 scopus 로고    scopus 로고
    • Growth and muscle defects in mice lacking adult myosin heavy chain genes
    • Acakpo-Satchivi L.J., et al. Growth and muscle defects in mice lacking adult myosin heavy chain genes. J. Cell Biol. 1997, 139:1219-1229.
    • (1997) J. Cell Biol. , vol.139 , pp. 1219-1229
    • Acakpo-Satchivi, L.J.1
  • 19
    • 0034256090 scopus 로고    scopus 로고
    • Calmodulin: a prototypical calcium sensor
    • Chin D., Means A.R. Calmodulin: a prototypical calcium sensor. Trends Cell Biol. 2000, 10:322-328.
    • (2000) Trends Cell Biol. , vol.10 , pp. 322-328
    • Chin, D.1    Means, A.R.2
  • 21
    • 0037462474 scopus 로고    scopus 로고
    • Sensing stretch is fundamental
    • Epstein N.D., Davis J.S. Sensing stretch is fundamental. Cell 2003, 112:147-150.
    • (2003) Cell , vol.112 , pp. 147-150
    • Epstein, N.D.1    Davis, J.S.2
  • 22
    • 2442481067 scopus 로고    scopus 로고
    • Alpha-actinin revisited: a fresh look at an old player
    • Otey C.A., Carpen O. Alpha-actinin revisited: a fresh look at an old player. Cell Motil. Cytoskeleton 2004, 58:104-111.
    • (2004) Cell Motil. Cytoskeleton , vol.58 , pp. 104-111
    • Otey, C.A.1    Carpen, O.2
  • 24
    • 0023653358 scopus 로고
    • Calcium-sensitive non-muscle alpha-actinin contains EF-hand structures and highly conserved regions
    • Noegel A., Witke W., Schleicher M. Calcium-sensitive non-muscle alpha-actinin contains EF-hand structures and highly conserved regions. FEBS Lett. 1987, 221:391-396.
    • (1987) FEBS Lett. , vol.221 , pp. 391-396
    • Noegel, A.1    Witke, W.2    Schleicher, M.3
  • 25
    • 0026756594 scopus 로고
    • Requirement of phosphatidylinositol 4, 5-bisphosphate for alpha-actinin function
    • Fukami K., Furuhashi K., Inagaki M., Endo T., Hatano S., Takenawa T. Requirement of phosphatidylinositol 4, 5-bisphosphate for alpha-actinin function. Nature 1992, 359:150-152.
    • (1992) Nature , vol.359 , pp. 150-152
    • Fukami, K.1    Furuhashi, K.2    Inagaki, M.3    Endo, T.4    Hatano, S.5    Takenawa, T.6
  • 26
    • 74949102278 scopus 로고    scopus 로고
    • The evolution of skeletal muscle performance: gene duplication and divergence of human sarcomeric alpha-actinins
    • Lek M., Quinlan K.G., North K.N. The evolution of skeletal muscle performance: gene duplication and divergence of human sarcomeric alpha-actinins. BioEssays 2010, 32:17-25.
    • (2010) BioEssays , vol.32 , pp. 17-25
    • Lek, M.1    Quinlan, K.G.2    North, K.N.3
  • 27
    • 77952300824 scopus 로고    scopus 로고
    • Phylogenetic analysis of gene structure and alternative splicing in alpha-actinins
    • Lek M., MacArthur D.G., Yang N., North K.N. Phylogenetic analysis of gene structure and alternative splicing in alpha-actinins. Mol. Biol. Evol. 2010, 27:773-780.
    • (2010) Mol. Biol. Evol. , vol.27 , pp. 773-780
    • Lek, M.1    MacArthur, D.G.2    Yang, N.3    North, K.N.4
  • 28
    • 0142058043 scopus 로고    scopus 로고
    • Mutations in the muscle LIM protein and alpha-actinin-2 genes in dilated cardiomyopathy and endocardial fibroelastosis
    • Mohapatra B., et al. Mutations in the muscle LIM protein and alpha-actinin-2 genes in dilated cardiomyopathy and endocardial fibroelastosis. Mol. Genet. Metab. 2003, 80:207-215.
    • (2003) Mol. Genet. Metab. , vol.80 , pp. 207-215
    • Mohapatra, B.1
  • 29
    • 4043152847 scopus 로고    scopus 로고
    • Decreased interactions of mutant muscle LIM protein (MLP) with N-RAP and alpha-actinin and their implication for hypertrophic cardiomyopathy
    • Gehmlich K., Geier C., Osterziel K.J., Van der Ven P.F., Furst D.O. Decreased interactions of mutant muscle LIM protein (MLP) with N-RAP and alpha-actinin and their implication for hypertrophic cardiomyopathy. Cell Tissue Res. 2004, 317:129-136.
    • (2004) Cell Tissue Res. , vol.317 , pp. 129-136
    • Gehmlich, K.1    Geier, C.2    Osterziel, K.J.3    Van der Ven, P.F.4    Furst, D.O.5
  • 30
    • 18444408379 scopus 로고    scopus 로고
    • Titin mutations as the molecular basis for dilated cardiomyopathy
    • Itoh-Satoh M., et al. Titin mutations as the molecular basis for dilated cardiomyopathy. Biochem. Biophys. Res. Commun. 2002, 291:385-393.
    • (2002) Biochem. Biophys. Res. Commun. , vol.291 , pp. 385-393
    • Itoh-Satoh, M.1
  • 31
    • 17944383882 scopus 로고    scopus 로고
    • The adenosine A2A receptor interacts with the actin-binding protein alpha-actinin
    • Burgueno J., et al. The adenosine A2A receptor interacts with the actin-binding protein alpha-actinin. J. Biol. Chem. 2003, 278:37545-37552.
    • (2003) J. Biol. Chem. , vol.278 , pp. 37545-37552
    • Burgueno, J.1
  • 32
    • 76949086546 scopus 로고    scopus 로고
    • Alpha-actinin interacts with rapsyn in agrin-stimulated AChR clustering
    • Dobbins G.C., Luo S., Yang Z., Xiong W.C., Mei L. Alpha-actinin interacts with rapsyn in agrin-stimulated AChR clustering. Mol. Brain 2008, 1:18.
    • (2008) Mol. Brain , vol.1 , pp. 18
    • Dobbins, G.C.1    Luo, S.2    Yang, Z.3    Xiong, W.C.4    Mei, L.5
  • 33
    • 0034640199 scopus 로고    scopus 로고
    • Alpha-actinin-2 couples to cardiac Kv1.5 channels, regulating current density and channel localization in HEK cells
    • Maruoka N.D., Steele D.F., Au B.P., Dan P., Zhang X., Moore E.D., Fedida D. Alpha-actinin-2 couples to cardiac Kv1.5 channels, regulating current density and channel localization in HEK cells. FEBS Lett. 2000, 473:188-194.
    • (2000) FEBS Lett. , vol.473 , pp. 188-194
    • Maruoka, N.D.1    Steele, D.F.2    Au, B.P.3    Dan, P.4    Zhang, X.5    Moore, E.D.6    Fedida, D.7
  • 34
    • 73449124479 scopus 로고    scopus 로고
    • Cell membrane expression of cardiac sodium channel Na(v)1.5 is modulated by alpha-actinin-2 interaction
    • Ziane R., Huang H., Moghadaszadeh B., Beggs A.H., Levesque G., Chahine M. Cell membrane expression of cardiac sodium channel Na(v)1.5 is modulated by alpha-actinin-2 interaction. Biochemistry 2010, 49:166-178.
    • (2010) Biochemistry , vol.49 , pp. 166-178
    • Ziane, R.1    Huang, H.2    Moghadaszadeh, B.3    Beggs, A.H.4    Levesque, G.5    Chahine, M.6
  • 35
    • 21244504957 scopus 로고    scopus 로고
    • Alpha-actinin associates with polycystin-2 and regulates its channel activity
    • Li Q., et al. Alpha-actinin associates with polycystin-2 and regulates its channel activity. Hum. Mol. Genet. 2005, 14:1587-1603.
    • (2005) Hum. Mol. Genet. , vol.14 , pp. 1587-1603
    • Li, Q.1
  • 36
    • 36448981005 scopus 로고    scopus 로고
    • Direct binding of alpha-actinin enhances TRPP3 channel activity
    • Li Q., et al. Direct binding of alpha-actinin enhances TRPP3 channel activity. J. Neurochem. 2007, 103:2391-2400.
    • (2007) J. Neurochem. , vol.103 , pp. 2391-2400
    • Li, Q.1
  • 37
    • 0036080358 scopus 로고    scopus 로고
    • Regulation of the cardiac L-type Ca2+ channel by the actin-binding proteins alpha-actinin and dystrophin
    • Sadeghi A., Doyle A.D., Johnson B.D. Regulation of the cardiac L-type Ca2+ channel by the actin-binding proteins alpha-actinin and dystrophin. Am. J. Physiol. Cell Physiol. 2002, 282:C1502-C1511.
    • (2002) Am. J. Physiol. Cell Physiol. , vol.282
    • Sadeghi, A.1    Doyle, A.D.2    Johnson, B.D.3
  • 38
    • 54449097591 scopus 로고    scopus 로고
    • Alpha-actinin-4 is selectively required for insulin-induced GLUT4 translocation
    • Talior-Volodarsky I., Randhawa V.K., Zaid H., Klip A. Alpha-actinin-4 is selectively required for insulin-induced GLUT4 translocation. J. Biol. Chem. 2008, 283:25115-25123.
    • (2008) J. Biol. Chem. , vol.283 , pp. 25115-25123
    • Talior-Volodarsky, I.1    Randhawa, V.K.2    Zaid, H.3    Klip, A.4
  • 39
    • 26844443598 scopus 로고    scopus 로고
    • Phosphorylation-dependent interactions of alpha-actinin-1/IQGAP1 with the AMPA receptor subunit GluR4
    • Nuriya M., Oh S., Huganir R.L. Phosphorylation-dependent interactions of alpha-actinin-1/IQGAP1 with the AMPA receptor subunit GluR4. J. Neurochem. 2005, 95:544-552.
    • (2005) J. Neurochem. , vol.95 , pp. 544-552
    • Nuriya, M.1    Oh, S.2    Huganir, R.L.3
  • 42
    • 0031013896 scopus 로고    scopus 로고
    • Competitive binding of alpha-actinin and calmodulin to the NMDA receptor
    • Wyszynski M., Lin J., Rao A., Nigh E., Beggs A.H., Craig A.M., Sheng M. Competitive binding of alpha-actinin and calmodulin to the NMDA receptor. Nature 1997, 385:439-442.
    • (1997) Nature , vol.385 , pp. 439-442
    • Wyszynski, M.1    Lin, J.2    Rao, A.3    Nigh, E.4    Beggs, A.H.5    Craig, A.M.6    Sheng, M.7
  • 43
    • 0037184992 scopus 로고    scopus 로고
    • The cardiac mechanical stretch sensor machinery involves a Z disc complex that is defective in a subset of human dilated cardiomyopathy
    • Knoll R., et al. The cardiac mechanical stretch sensor machinery involves a Z disc complex that is defective in a subset of human dilated cardiomyopathy. Cell 2002, 111:943-955.
    • (2002) Cell , vol.111 , pp. 943-955
    • Knoll, R.1
  • 44
    • 50849138457 scopus 로고    scopus 로고
    • Beyond the sarcomere: CSRP3 mutations cause hypertrophic cardiomyopathy
    • Geier C., et al. Beyond the sarcomere: CSRP3 mutations cause hypertrophic cardiomyopathy. Hum. Mol. Genet. 2008, 17:2753-2765.
    • (2008) Hum. Mol. Genet. , vol.17 , pp. 2753-2765
    • Geier, C.1
  • 45
    • 69249246979 scopus 로고    scopus 로고
    • Myocyte remodeling in response to hypertrophic stimuli requires nucleocytoplasmic shuttling of muscle LIM protein
    • Boateng S.Y., Senyo S.E., Qi L., Goldspink P.H., Russell B. Myocyte remodeling in response to hypertrophic stimuli requires nucleocytoplasmic shuttling of muscle LIM protein. J. Mol. Cell. Cardiol. 2009, 47:426-435.
    • (2009) J. Mol. Cell. Cardiol. , vol.47 , pp. 426-435
    • Boateng, S.Y.1    Senyo, S.E.2    Qi, L.3    Goldspink, P.H.4    Russell, B.5
  • 46
    • 0030760375 scopus 로고    scopus 로고
    • CRP1, a LIM domain protein implicated in muscle differentiation, interacts with alpha-actinin
    • Pomies P., Louis H.A., Beckerle M.C. CRP1, a LIM domain protein implicated in muscle differentiation, interacts with alpha-actinin. J. Cell Biol. 1997, 139:157-168.
    • (1997) J. Cell Biol. , vol.139 , pp. 157-168
    • Pomies, P.1    Louis, H.A.2    Beckerle, M.C.3
  • 47
    • 0030933063 scopus 로고    scopus 로고
    • MLP-deficient mice exhibit a disruption of cardiac cytoarchitectural organization, dilated cardiomyopathy, and heart failure
    • Arber S., et al. MLP-deficient mice exhibit a disruption of cardiac cytoarchitectural organization, dilated cardiomyopathy, and heart failure. Cell 1997, 88:393-403.
    • (1997) Cell , vol.88 , pp. 393-403
    • Arber, S.1
  • 48
    • 0028073676 scopus 로고
    • Muscle LIM protein, a novel essential regulator of myogenesis, promotes myogenic differentiation
    • Arber S., Halder G., Caroni P. Muscle LIM protein, a novel essential regulator of myogenesis, promotes myogenic differentiation. Cell 1994, 79:221-231.
    • (1994) Cell , vol.79 , pp. 221-231
    • Arber, S.1    Halder, G.2    Caroni, P.3
  • 49
    • 77649218547 scopus 로고    scopus 로고
    • Mutations in alpha-actinin-2 cause hypertrophic cardiomyopathy: a genome-wide analysis
    • Chiu C., et al. Mutations in alpha-actinin-2 cause hypertrophic cardiomyopathy: a genome-wide analysis. J. Am. Coll. Cardiol. 2010, 55:1127-1135.
    • (2010) J. Am. Coll. Cardiol. , vol.55 , pp. 1127-1135
    • Chiu, C.1
  • 50
    • 0033519274 scopus 로고    scopus 로고
    • Myogenin induces a shift of enzyme activity from glycolytic to oxidative metabolism in muscles of transgenic mice
    • Hughes S.M., Chi M.M., Lowry O.H., Gundersen K. Myogenin induces a shift of enzyme activity from glycolytic to oxidative metabolism in muscles of transgenic mice. J. Cell Biol. 1999, 145:633-642.
    • (1999) J. Cell Biol. , vol.145 , pp. 633-642
    • Hughes, S.M.1    Chi, M.M.2    Lowry, O.H.3    Gundersen, K.4
  • 52
    • 0034120259 scopus 로고    scopus 로고
    • Remodeling muscles with calcineurin
    • Olson E.N., Williams R.S. Remodeling muscles with calcineurin. BioEssays 2000, 22:510-519.
    • (2000) BioEssays , vol.22 , pp. 510-519
    • Olson, E.N.1    Williams, R.S.2
  • 53
    • 0037134462 scopus 로고    scopus 로고
    • Calsarcin-3, a novel skeletal muscle-specific member of the calsarcin family, interacts with multiple Z-disc proteins
    • Frey N., Olson E.N. Calsarcin-3, a novel skeletal muscle-specific member of the calsarcin family, interacts with multiple Z-disc proteins. J. Biol. Chem. 2002, 277:13998-14004.
    • (2002) J. Biol. Chem. , vol.277 , pp. 13998-14004
    • Frey, N.1    Olson, E.N.2
  • 54
    • 0034731460 scopus 로고    scopus 로고
    • FATZ, a filamin-, actinin-, and telethonin-binding protein of the Z-disc of skeletal muscle
    • Faulkner G., et al. FATZ, a filamin-, actinin-, and telethonin-binding protein of the Z-disc of skeletal muscle. J. Biol. Chem. 2000, 275:41234-41242.
    • (2000) J. Biol. Chem. , vol.275 , pp. 41234-41242
    • Faulkner, G.1
  • 56
    • 0034687814 scopus 로고    scopus 로고
    • Calsarcins, a novel family of sarcomeric calcineurin-binding proteins
    • Frey N., Richardson J.A., Olson E.N. Calsarcins, a novel family of sarcomeric calcineurin-binding proteins. Proc. Natl. Acad. Sci. USA 2000, 97:14632-14637.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 14632-14637
    • Frey, N.1    Richardson, J.A.2    Olson, E.N.3
  • 57
    • 19944423058 scopus 로고    scopus 로고
    • Mice lacking calsarcin-1 are sensitized to calcineurin signaling and show accelerated cardiomyopathy in response to pathological biomechanical stress
    • Frey N., et al. Mice lacking calsarcin-1 are sensitized to calcineurin signaling and show accelerated cardiomyopathy in response to pathological biomechanical stress. Nat. Med. 2004, 10:1336-1343.
    • (2004) Nat. Med. , vol.10 , pp. 1336-1343
    • Frey, N.1
  • 58
    • 55849135238 scopus 로고    scopus 로고
    • Calsarcin-2 deficiency increases exercise capacity in mice through calcineurin/NFAT activation
    • Frey N., et al. Calsarcin-2 deficiency increases exercise capacity in mice through calcineurin/NFAT activation. J. Clin. Invest. 2008, 118:3598-3608.
    • (2008) J. Clin. Invest. , vol.118 , pp. 3598-3608
    • Frey, N.1
  • 59
    • 59249091710 scopus 로고    scopus 로고
    • A class III PDZ binding motif in the myotilin and FATZ families binds enigma family proteins: a common link for Z-disc myopathies
    • von Nandelstadh P., et al. A class III PDZ binding motif in the myotilin and FATZ families binds enigma family proteins: a common link for Z-disc myopathies. Mol. Cell Biol. 2009, 29:822-834.
    • (2009) Mol. Cell Biol. , vol.29 , pp. 822-834
    • von Nandelstadh, P.1
  • 60
    • 11144356337 scopus 로고    scopus 로고
    • Foxo transcription factors induce the atrophy-related ubiquitin ligase atrogin-1 and cause skeletal muscle atrophy
    • Sandri M., et al. Foxo transcription factors induce the atrophy-related ubiquitin ligase atrogin-1 and cause skeletal muscle atrophy. Cell 2004, 117:399-412.
    • (2004) Cell , vol.117 , pp. 399-412
    • Sandri, M.1
  • 61
    • 0035941020 scopus 로고    scopus 로고
    • Identification of ubiquitin ligases required for skeletal muscle atrophy
    • Bodine S.C., et al. Identification of ubiquitin ligases required for skeletal muscle atrophy. Science 2001, 294:1704-1708.
    • (2001) Science , vol.294 , pp. 1704-1708
    • Bodine, S.C.1
  • 62
    • 9644270401 scopus 로고    scopus 로고
    • Atrogin-1/muscle atrophy F-box inhibits calcineurin-dependent cardiac hypertrophy by participating in an SCF ubiquitin ligase complex
    • Li H.H., Kedar V., Zhang C., McDonough H., Arya R., Wang D.Z., Patterson C. Atrogin-1/muscle atrophy F-box inhibits calcineurin-dependent cardiac hypertrophy by participating in an SCF ubiquitin ligase complex. J. Clin. Invest. 2004, 114:1058-1071.
    • (2004) J. Clin. Invest. , vol.114 , pp. 1058-1071
    • Li, H.H.1    Kedar, V.2    Zhang, C.3    McDonough, H.4    Arya, R.5    Wang, D.Z.6    Patterson, C.7
  • 64
    • 69249222488 scopus 로고    scopus 로고
    • Identification of MAFbx as a myogenin-engaged F-box protein in SCF ubiquitin ligase
    • Jogo M., Shiraishi S., Tamura T.A. Identification of MAFbx as a myogenin-engaged F-box protein in SCF ubiquitin ligase. FEBS Lett. 2009, 583:2715-2719.
    • (2009) FEBS Lett. , vol.583 , pp. 2715-2719
    • Jogo, M.1    Shiraishi, S.2    Tamura, T.A.3
  • 65
    • 0021129923 scopus 로고
    • Interactions between glycolytic enzymes and components of the cytomatrix
    • Masters C. Interactions between glycolytic enzymes and components of the cytomatrix. J. Cell Biol. 1984, 99:222s-225s.
    • (1984) J. Cell Biol. , vol.99
    • Masters, C.1
  • 66
    • 0034494381 scopus 로고    scopus 로고
    • Coupling of creatine kinase to glycolytic enzymes at the sarcomeric I-band of skeletal muscle: a biochemical study in situ
    • Kraft T., Hornemann T., Stolz M., Nier V., Wallimann T. Coupling of creatine kinase to glycolytic enzymes at the sarcomeric I-band of skeletal muscle: a biochemical study in situ. J. Muscle Res. Cell Motil. 2000, 21:691-703.
    • (2000) J. Muscle Res. Cell Motil. , vol.21 , pp. 691-703
    • Kraft, T.1    Hornemann, T.2    Stolz, M.3    Nier, V.4    Wallimann, T.5
  • 67
    • 0242299766 scopus 로고    scopus 로고
    • Colocalization of muscle FBPase and muscle aldolase on both sides of the Z-line
    • Rakus D., Mamczur P., Gizak A., Dus D., Dzugaj A. Colocalization of muscle FBPase and muscle aldolase on both sides of the Z-line. Biochem. Biophys. Res. Commun. 2003, 311:294-299.
    • (2003) Biochem. Biophys. Res. Commun. , vol.311 , pp. 294-299
    • Rakus, D.1    Mamczur, P.2    Gizak, A.3    Dus, D.4    Dzugaj, A.5
  • 68
    • 0036786003 scopus 로고    scopus 로고
    • Amorphin is phosphorylase; phosphorylase is an alpha-actinin-binding protein
    • Chowrashi P., Mittal B., Sanger J.M., Sanger J.W. Amorphin is phosphorylase; phosphorylase is an alpha-actinin-binding protein. Cell Motil. Cytoskeleton 2002, 53:125-135.
    • (2002) Cell Motil. Cytoskeleton , vol.53 , pp. 125-135
    • Chowrashi, P.1    Mittal, B.2    Sanger, J.M.3    Sanger, J.W.4
  • 69
    • 0024393117 scopus 로고
    • Subcellular localization of glycogen synthase with monoclonal antibodies
    • Lane R.D., Hegazy M.G., Reimann E.M. Subcellular localization of glycogen synthase with monoclonal antibodies. Biochem. Int. 1989, 18:961-970.
    • (1989) Biochem. Int. , vol.18 , pp. 961-970
    • Lane, R.D.1    Hegazy, M.G.2    Reimann, E.M.3
  • 70
    • 14844330060 scopus 로고    scopus 로고
    • The effect of calcium ions on subcellular localization of aldolase-FBPase complex in skeletal muscle
    • Mamczur P., Rakus D., Gizak A., Dus D., Dzugaj A. The effect of calcium ions on subcellular localization of aldolase-FBPase complex in skeletal muscle. FEBS Lett. 2005, 579:1607-1612.
    • (2005) FEBS Lett. , vol.579 , pp. 1607-1612
    • Mamczur, P.1    Rakus, D.2    Gizak, A.3    Dus, D.4    Dzugaj, A.5
  • 71
    • 0037478975 scopus 로고    scopus 로고
    • Muscle FBPase in a complex with muscle aldolase is insensitive to AMP inhibition
    • Rakus D., Pasek M., Krotkiewski H., Dzugaj A. Muscle FBPase in a complex with muscle aldolase is insensitive to AMP inhibition. FEBS Lett. 2003, 547:11-14.
    • (2003) FEBS Lett. , vol.547 , pp. 11-14
    • Rakus, D.1    Pasek, M.2    Krotkiewski, H.3    Dzugaj, A.4
  • 72
    • 9744229890 scopus 로고    scopus 로고
    • Interaction between muscle aldolase and muscle fructose 1,6-bisphosphatase results in the substrate channeling
    • Rakus D., Pasek M., Krotkiewski H., Dzugaj A. Interaction between muscle aldolase and muscle fructose 1,6-bisphosphatase results in the substrate channeling. Biochemistry 2004, 43:14948-14957.
    • (2004) Biochemistry , vol.43 , pp. 14948-14957
    • Rakus, D.1    Pasek, M.2    Krotkiewski, H.3    Dzugaj, A.4
  • 73
    • 34447098032 scopus 로고    scopus 로고
    • Colocalization of aldolase and FBPase in cytoplasm and nucleus of cardiomyocytes
    • Mamczur P., Dus D., Dzugaj A. Colocalization of aldolase and FBPase in cytoplasm and nucleus of cardiomyocytes. Cell Biol. Int. 2007, 31:1122-1130.
    • (2007) Cell Biol. Int. , vol.31 , pp. 1122-1130
    • Mamczur, P.1    Dus, D.2    Dzugaj, A.3
  • 74
    • 33745860355 scopus 로고    scopus 로고
    • Changes in subcellular localization of fructose 1,6-bisphosphatase during differentiation of isolated muscle satellite cells
    • Gizak A., Wrobel E., Moraczewski J., Dzugaj A. Changes in subcellular localization of fructose 1,6-bisphosphatase during differentiation of isolated muscle satellite cells. FEBS Lett. 2006, 580:4042-4046.
    • (2006) FEBS Lett. , vol.580 , pp. 4042-4046
    • Gizak, A.1    Wrobel, E.2    Moraczewski, J.3    Dzugaj, A.4
  • 75
    • 26244450185 scopus 로고    scopus 로고
    • Nuclear localization of fructose 1,6-bisphosphatase in smooth muscle cells
    • Gizak A., Rakus D., Dzugaj A. Nuclear localization of fructose 1,6-bisphosphatase in smooth muscle cells. J. Mol. Histol. 2005, 36:243-248.
    • (2005) J. Mol. Histol. , vol.36 , pp. 243-248
    • Gizak, A.1    Rakus, D.2    Dzugaj, A.3
  • 76
    • 70349446515 scopus 로고    scopus 로고
    • Muscle FBPase is targeted to nucleus by its 203KKKGK207 sequence
    • Gizak A., Maciaszczyk-Dziubinska E., Jurowicz M., Rakus D. Muscle FBPase is targeted to nucleus by its 203KKKGK207 sequence. Proteins 2009, 77:262-267.
    • (2009) Proteins , vol.77 , pp. 262-267
    • Gizak, A.1    Maciaszczyk-Dziubinska, E.2    Jurowicz, M.3    Rakus, D.4
  • 78
    • 0018676274 scopus 로고
    • Glycogen synthesis from lactate in the three types of skeletal muscle
    • McLane J.A., Holloszy J.O. Glycogen synthesis from lactate in the three types of skeletal muscle. J. Biol. Chem. 1979, 254:6548-6553.
    • (1979) J. Biol. Chem. , vol.254 , pp. 6548-6553
    • McLane, J.A.1    Holloszy, J.O.2
  • 79
    • 44949168573 scopus 로고    scopus 로고
    • Evolutionary conserved N-terminal region of human muscle fructose 1,6-bisphosphatase regulates its activity and the interaction with aldolase
    • Gizak A., Maciaszczyk E., Dzugaj A., Eschrich K., Rakus D. Evolutionary conserved N-terminal region of human muscle fructose 1,6-bisphosphatase regulates its activity and the interaction with aldolase. Proteins 2008, 72:209-216.
    • (2008) Proteins , vol.72 , pp. 209-216
    • Gizak, A.1    Maciaszczyk, E.2    Dzugaj, A.3    Eschrich, K.4    Rakus, D.5
  • 80
    • 36348972777 scopus 로고    scopus 로고
    • Overexpression of the cytosolic form of phosphoenolpyruvate carboxykinase (GTP) in skeletal muscle repatterns energy metabolism in the mouse
    • Hakimi P., et al. Overexpression of the cytosolic form of phosphoenolpyruvate carboxykinase (GTP) in skeletal muscle repatterns energy metabolism in the mouse. J. Biol. Chem. 2007, 282:32844-32855.
    • (2007) J. Biol. Chem. , vol.282 , pp. 32844-32855
    • Hakimi, P.1
  • 81
    • 36849051314 scopus 로고    scopus 로고
    • Protein kinase A, Ca2+/calmodulin-dependent kinase II, and calcineurin regulate the intracellular trafficking of myopodin between the Z-disc and the nucleus of cardiac myocytes
    • Faul C., Dhume A., Schecter A.D., Mundel P. Protein kinase A, Ca2+/calmodulin-dependent kinase II, and calcineurin regulate the intracellular trafficking of myopodin between the Z-disc and the nucleus of cardiac myocytes. Mol. Cell Biol. 2007, 27:8215-8227.
    • (2007) Mol. Cell Biol. , vol.27 , pp. 8215-8227
    • Faul, C.1    Dhume, A.2    Schecter, A.D.3    Mundel, P.4
  • 82
    • 0038605975 scopus 로고    scopus 로고
    • FHL3 is an actin-binding protein that regulates alpha-actinin-mediated actin bundling: FHL3 localizes to actin stress fibers and enhances cell spreading and stress fiber disassembly
    • Coghill I.D., Brown S., Cottle D.L., McGrath M.J., Robinson P.A., Nandurkar H.H., Dyson J.M., Mitchell C.A. FHL3 is an actin-binding protein that regulates alpha-actinin-mediated actin bundling: FHL3 localizes to actin stress fibers and enhances cell spreading and stress fiber disassembly. J. Biol. Chem. 2003, 278:24139-24152.
    • (2003) J. Biol. Chem. , vol.278 , pp. 24139-24152
    • Coghill, I.D.1    Brown, S.2    Cottle, D.L.3    McGrath, M.J.4    Robinson, P.A.5    Nandurkar, H.H.6    Dyson, J.M.7    Mitchell, C.A.8
  • 83
    • 33846017683 scopus 로고    scopus 로고
    • Myomaxin is a novel transcriptional target of MEF2A that encodes a Xin-related alpha-actinin-interacting protein
    • Huang H.T., Brand O.M., Mathew M., Ignatiou C., Ewen E.P., McCalmon S.A., Naya F.J. Myomaxin is a novel transcriptional target of MEF2A that encodes a Xin-related alpha-actinin-interacting protein. J. Biol. Chem. 2006, 281:39370-39379.
    • (2006) J. Biol. Chem. , vol.281 , pp. 39370-39379
    • Huang, H.T.1    Brand, O.M.2    Mathew, M.3    Ignatiou, C.4    Ewen, E.P.5    McCalmon, S.A.6    Naya, F.J.7
  • 84
    • 33646559605 scopus 로고    scopus 로고
    • Myospryn is a direct transcriptional target for MEF2A that encodes a striated muscle, alpha-actinin-interacting, costamere-localized protein
    • Durham J.T., Brand O.M., Arnold M., Reynolds J.G., Muthukumar L., Weiler H., Richardson J.A., Naya F.J. Myospryn is a direct transcriptional target for MEF2A that encodes a striated muscle, alpha-actinin-interacting, costamere-localized protein. J. Biol. Chem. 2006, 281:6841-6849.
    • (2006) J. Biol. Chem. , vol.281 , pp. 6841-6849
    • Durham, J.T.1    Brand, O.M.2    Arnold, M.3    Reynolds, J.G.4    Muthukumar, L.5    Weiler, H.6    Richardson, J.A.7    Naya, F.J.8
  • 85
    • 1842737542 scopus 로고    scopus 로고
    • Evidence for myofibril remodeling as opposed to myofibril damage in human muscles with DOMS: an ultrastructural and immunoelectron microscopic study
    • Yu J.G., Carlsson L., Thornell L.E. Evidence for myofibril remodeling as opposed to myofibril damage in human muscles with DOMS: an ultrastructural and immunoelectron microscopic study. Histochem. Cell Biol. 2004, 121:219-227.
    • (2004) Histochem. Cell Biol. , vol.121 , pp. 219-227
    • Yu, J.G.1    Carlsson, L.2    Thornell, L.E.3
  • 86
    • 0030848969 scopus 로고    scopus 로고
    • Utrophin-dystrophin-deficient mice as a model for Duchenne muscular dystrophy
    • Deconinck A.E., et al. Utrophin-dystrophin-deficient mice as a model for Duchenne muscular dystrophy. Cell 1997, 90:717-727.
    • (1997) Cell , vol.90 , pp. 717-727
    • Deconinck, A.E.1
  • 87
    • 66349112238 scopus 로고    scopus 로고
    • Rescue of skeletal muscle alpha-actin-null mice by cardiac (fetal) alpha-actin
    • Nowak K.J., et al. Rescue of skeletal muscle alpha-actin-null mice by cardiac (fetal) alpha-actin. J. Cell Biol. 2009, 185:903-915.
    • (2009) J. Cell Biol. , vol.185 , pp. 903-915
    • Nowak, K.J.1


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