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Volumn 29, Issue 22, 2009, Pages 6046-6058

Muscle Lim protein interacts with cofilin 2 and regulates F-actin dynamics in cardiac and skeletal muscle

Author keywords

[No Author keywords available]

Indexed keywords

COFILIN 2; F ACTIN; LIM PROTEIN;

EID: 71949112812     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.00654-09     Document Type: Article
Times cited : (50)

References (89)
  • 1
    • 0027243449 scopus 로고
    • Cytoplasmic localization and nuclear transport of cofilin in cultured myotubes
    • Abe, H., R. Nagaoka, and T. Obinata. 1993. Cytoplasmic localization and nuclear transport of cofilin in cultured myotubes. Exp. Cell Res. 206:1-10.
    • (1993) Exp. Cell Res. , vol.206 , pp. 1-10
    • Abe, H.1    Nagaoka, R.2    Obinata, T.3
  • 2
    • 0029149885 scopus 로고
    • Reactivation of phosphorylated actin depolymerizing factor and identification of the regulatory site
    • Agnew, B. J., L. S. Minamide, and J. R. Bamburg. 1995. Reactivation of phosphorylated actin depolymerizing factor and identification of the regulatory site. J. Biol. Chem. 270:17582-17587.
    • (1995) J. Biol. Chem. , vol.270 , pp. 17582-17587
    • Agnew, B.J.1    Minamide, L.S.2    Bamburg, J.R.3
  • 4
    • 4544242249 scopus 로고    scopus 로고
    • Stretch of the vascular wall induces smooth muscle differentiation by promoting actin polymerization
    • Albinsson, S., I. Nordstrom, and P. Hellstrand. 2004. Stretch of the vascular wall induces smooth muscle differentiation by promoting actin polymerization. J. Biol. Chem. 279:34849-34855.
    • (2004) J. Biol. Chem. , vol.279 , pp. 34849-34855
    • Albinsson, S.1    Nordstrom, I.2    Hellstrand, P.3
  • 5
    • 0034536444 scopus 로고    scopus 로고
    • The serine phosphatases PP1 and PP2A associate with and activate the actin-binding protein cofilin in human T lymphocytes
    • Ambach, A., J. Saunus, M. Konstandin, S. Wesselborg, S. C. Meuer, and Y. Samstag. 2000. The serine phosphatases PP1 and PP2A associate with and activate the actin-binding protein cofilin in human T lymphocytes. Eur. J. Immunol. 30:3422-3431.
    • (2000) Eur. J. Immunol. , vol.30 , pp. 3422-3431
    • Ambach, A.1    Saunus, J.2    Konstandin, M.3    Wesselborg, S.4    Meuer, S.C.5    Samstag, Y.6
  • 6
    • 0032565962 scopus 로고    scopus 로고
    • Regulation of actin dynamics through phosphorylation of cofilin by LIM- Kinase
    • DOI 10.1038/31729
    • Arber, S., F. A. Barbayannis, H. Hanser, C. Schneider, C. A. Stanyon, O. Bernard, and P. Caroni. 1998. Regulation of actin dynamics through phosphorylation of cofilin by LIM-kinase. Nature 393:805-809. (Pubitemid 28299494)
    • (1998) Nature , vol.393 , Issue.6687 , pp. 805-809
    • Arber, S.1    Barbayannis, F.A.2    Hanser, H.3    Schnelder, C.4    Stanyon, C.A.5    Bernards, O.6    Caroni, P.7
  • 7
    • 0030024632 scopus 로고    scopus 로고
    • Specificity of single LIM motifs in targeting and LIM/LIM interactions in situ
    • Arber, S., and P. Caroni. 1996. Specificity of single LIM motifs in targeting and LIM/LIM interactions in situ. Genes Dev. 10:289-300. (Pubitemid 26058962)
    • (1996) Genes and Development , vol.10 , Issue.3 , pp. 289-300
    • Arber, S.1    Caroni, P.2
  • 8
    • 0028073676 scopus 로고
    • Muscle LIM protein, a novel essential regulator of myogenesis, promotes myogenic differentiation
    • DOI 10.1016/0092-8674(94)90192-9
    • Arber, S., G. Halder, and P. Caroni. 1994. Muscle LIM protein, a novel essential regulator of myogenesis, promotes myogenic differentiation. Cell 79:221-231. (Pubitemid 24324913)
    • (1994) Cell , vol.79 , Issue.2 , pp. 221-231
    • Arber, S.1    Halder, G.2    Caroni, P.3
  • 9
    • 0030933063 scopus 로고    scopus 로고
    • MLP-deficient mice exhibit a disruption of cardiac cytoarchitectural organization, dilated cardiomyopathy, and heart failure
    • DOI 10.1016/S0092-8674(00)81878-4
    • Arber, S., J. J. Hunter, J. Ross, Jr., M. Hongo, G. Sansig, J. Borg, J. C. Perriard, K. R. Chien, and P. Caroni. 1997. MLP-deficient mice exhibit a disruption of cardiac cytoarchitectural organization, dilated cardiomyopathy, and heart failure. Cell 88:393-403. (Pubitemid 27131381)
    • (1997) Cell , vol.88 , Issue.3 , pp. 393-403
    • Arber, S.1    Hunter, J.J.2    Ross Jr., J.3    Hongo, M.4    Sansig, G.5    Borg, J.6    Perriard, J.-C.7    Chien, K.R.8    Caroni, P.9
  • 12
    • 0028348589 scopus 로고
    • Relaxation in ferret ventricular myocytes: Unusual interplay among calcium transport systems
    • Bassani, R. A., J. W. Bassani, and D. M. Bers. 1994. Relaxation in ferret ventricular myocytes: unusual interplay among calcium transport systems. J. Physiol. 476:295-308.
    • (1994) J. Physiol. , vol.476 , pp. 295-308
    • Bassani, R.A.1    Bassani, J.W.2    Bers, D.M.3
  • 15
    • 0034801641 scopus 로고    scopus 로고
    • Cofilin activation during Ca(2+)-triggered secretion from adrenal chromaffin cells
    • Birkenfeld, J., B. Kartmann, H. Betz, and D. Roth. 2001. Cofilin activation during Ca(2+)-triggered secretion from adrenal chromaffin cells. Biochem. Biophys. Res. Commun. 286:493-498.
    • (2001) Biochem. Biophys. Res. Commun. , vol.286 , pp. 493-498
    • Birkenfeld, J.1    Kartmann, B.2    Betz, H.3    Roth, D.4
  • 17
    • 0038071838 scopus 로고    scopus 로고
    • Actin-based motility as a self-organized system: Mechanism and reconstitution in vitro
    • Carlier, M. F., S. Wiesner, C. Le Clainche, and D. Pantaloni. 2003. Actin-based motility as a self-organized system: mechanism and reconstitution in vitro. C. R. Biol. 326:161-170.
    • (2003) C. R. Biol. , vol.326 , pp. 161-170
    • Carlier, M.F.1    Wiesner, S.2    Le Clainche, C.3    Pantaloni, D.4
  • 18
    • 2642580847 scopus 로고    scopus 로고
    • In vitro activity differences between proteins of the ADF/cofilin family define two distinct subgroups
    • Chen, H., B. W. Bernstein, J. M. Sneider, J. A. Boyle, L. S. Minamide, and J. R. Bamburg. 2004. In vitro activity differences between proteins of the ADF/cofilin family define two distinct subgroups. Biochemistry 43:7127-7142.
    • (2004) Biochemistry , vol.43 , pp. 7127-7142
    • Chen, H.1    Bernstein, B.W.2    Sneider, J.M.3    Boyle, J.A.4    Minamide, L.S.5    Bamburg, J.R.6
  • 19
    • 0025295430 scopus 로고
    • Specific association of calmodulin-dependent protein kinase and related substrates with the junctional sarcoplasmic reticulum of skeletal muscle
    • DOI 10.1021/bi00477a003
    • Chu, A., C. Sumbilla, G. Inesi, S. D. Jay, and K. P. Campbell. 1990. Specific association of calmodulin-dependent protein kinase and related substrates with the junctional sarcoplasmic reticulum of skeletal muscle. Biochemistry 29:5899-5905. (Pubitemid 20201390)
    • (1990) Biochemistry , vol.29 , Issue.25 , pp. 5899-5905
    • Chu, A.1    Sumbilla, C.2    Inesi, G.3    Jay, S.D.4    Campbell, K.P.5
  • 20
    • 33947582886 scopus 로고    scopus 로고
    • Sodium-hydrogen exchanger, cardiac overload, and myocardial hypertrophy
    • DOI 10.1161/CIRCULATIONAHA.106.626929, PII 0000301720070306000007
    • Cingolani, H. E., and I. L. Ennis. 2007. Sodium-hydrogen exchanger, cardiac overload, and myocardial hypertrophy. Circulation 115:1090-1100. (Pubitemid 46673171)
    • (2007) Circulation , vol.115 , Issue.9 , pp. 1090-1100
    • Cingolani, H.E.1    Ennis, I.L.2
  • 21
    • 0023195370 scopus 로고
    • Coronary sinus pH during percutaneous transluminal coronary angioplasty: Early development of acidosis during myocardial ischaemia in man
    • Crake, T., P. A. Crean, L. M. Shapiro, A. F. Rickards, and P. A. Poole- Wilson. 1987. Coronary sinus pH during percutaneous transluminal coronary angioplasty: early development of acidosis during myocardial ischaemia in man. Br. Heart J. 58:110-115.
    • (1987) Br. Heart J. , vol.58 , pp. 110-115
    • Crake, T.1    Crean, P.A.2    Shapiro, L.M.3    Rickards, A.F.4    Poole- Wilson, P.A.5
  • 22
    • 33646130148 scopus 로고    scopus 로고
    • Upregulation of profilin, cofilin-2 and LIMK2 in cultured pulmonary artery smooth muscle cells and in pulmonary arteries of monocrotaline-treated rats
    • Dai, Y. P., S. Bongalon, H. Tian, S. D. Parks, V. N. Mutafova-Yambolieva, and I. A. Yamboliev. 2006. Upregulation of profilin, cofilin-2 and LIMK2 in cultured pulmonary artery smooth muscle cells and in pulmonary arteries of monocrotaline-treated rats. Vascul. Pharmacol. 44:275-282.
    • (2006) Vascul. Pharmacol. , vol.44 , pp. 275-282
    • Dai, Y.P.1    Bongalon, S.2    Tian, H.3    Parks, S.D.4    Mutafova-Yambolieva, V.N.5    Yamboliev, I.A.6
  • 23
    • 0028286061 scopus 로고
    • Dephosphorylation of cofilin in stimulated platelets: Roles for a GTP-binding protein and Ca2+
    • Davidson, M. M., and R. J. Haslam. 1994. Dephosphorylation of cofilin in stimulated platelets: roles for a GTP-binding protein and Ca2+. Biochem. J. 301:41-47.
    • (1994) Biochem. J. , vol.301 , pp. 41-47
    • Davidson, M.M.1    Haslam, R.J.2
  • 24
    • 0034509337 scopus 로고    scopus 로고
    • Downregulation and nuclear relocation of MLP during the progression of right ventricular hypertrophy induced by chronic pressure overload
    • Ecarnot-Laubriet, A., K. De Luca, D. Vandroux, M. Moisant, C. Bernard, M. Assem, L. Rochette, and J. R. Teyssier. 2000. Downregulation and nuclear relocation of MLP during the progression of right ventricular hypertrophy induced by chronic pressure overload. J. Mol. Cell Cardiol. 32:2385-2395.
    • (2000) J. Mol. Cell Cardiol. , vol.32 , pp. 2385-2395
    • Ecarnot-Laubriet, A.1    De Luca, K.2    Vandroux, D.3    Moisant, M.4    Bernard, C.5    Assem, M.6    Rochette, L.7    Teyssier, J.R.8
  • 26
    • 0017345293 scopus 로고
    • Calcium release from the sarcoplasmic reticulum
    • Fabiato, A., and F. Fabiato. 1977. Calcium release from the sarcoplasmic reticulum. Circ. Res. 40:119-129.
    • (1977) Circ. Res. , vol.40 , pp. 119-129
    • Fabiato, A.1    Fabiato, F.2
  • 27
    • 0034025435 scopus 로고    scopus 로고
    • The muscle regulatory and structural protein MLP is a cytoskeletal binding partner of betaI-spectrin
    • Flick, M. J., and S. F. Konieczny. 2000. The muscle regulatory and structural protein MLP is a cytoskeletal binding partner of betaI-spectrin. J. Cell Sci. 113:1553-1564.
    • (2000) J. Cell Sci. , vol.113 , pp. 1553-1564
    • Flick, M.J.1    Konieczny, S.F.2
  • 29
    • 62449236060 scopus 로고    scopus 로고
    • Back to square one: What do we know about the functions of muscle LIM protein in the heart?
    • Gehmlich, K., C. Geier, H. Milting, D. Furst, and E. Ehler. 2008. Back to square one: what do we know about the functions of muscle LIM protein in the heart? J. Muscle Res. Cell Motil. 29:155-158.
    • (2008) J. Muscle Res. Cell Motil. , vol.29 , pp. 155-158
    • Gehmlich, K.1    Geier, C.2    Milting, H.3    Furst, D.4    Ehler, E.5
  • 30
    • 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., C. Geier, K. J. Osterziel, P. F. Van der Ven, and D. O. Furst. 2004. Decreased interactions of mutant muscle LIM protein (MLP) with N-RAP and alpha-actinin and their implication for hypertrophic cardiomyopathy. Cell Tissue Res. 317:129-136. (Pubitemid 39070612)
    • (2004) Cell and Tissue Research , vol.317 , Issue.2 , pp. 129-136
    • Gehmlich, K.1    Geier, C.2    Osterziel, K.J.3    Van Der Ven, P.F.M.4    Furst, D.O.5
  • 33
    • 12344250639 scopus 로고    scopus 로고
    • Chronophin, a novel HAD-type serine protein phosphatase, regulates cofilin-dependent actin dynamics
    • Gohla, A., J. Birkenfeld, and G. M. Bokoch. 2005. Chronophin, a novel HAD-type serine protein phosphatase, regulates cofilin-dependent actin dynamics. Nat. Cell Biol. 7:21-29.
    • (2005) Nat. Cell Biol. , vol.7 , pp. 21-29
    • Gohla, A.1    Birkenfeld, J.2    Bokoch, G.M.3
  • 34
    • 33750977562 scopus 로고    scopus 로고
    • Mapping the phosphoinositide- binding site on chick cofilin explains how PIP2 regulates the cofilin-actin interaction
    • Gorbatyuk, V. Y., N. J. Nosworthy, S. A. Robson, N. P. Bains, M. W. Maciejewski, C. G. Dos Remedios, and G. F. King. 2006. Mapping the phosphoinositide- binding site on chick cofilin explains how PIP2 regulates the cofilin-actin interaction. Mol. Cell 24:511-522.
    • (2006) Mol. Cell , vol.24 , pp. 511-522
    • Gorbatyuk, V.Y.1    Nosworthy, N.J.2    Robson, S.A.3    Bains, N.P.4    Maciejewski, M.W.5    Dos Remedios, C.G.6    King, G.F.7
  • 35
    • 1642573172 scopus 로고    scopus 로고
    • CRP2 is an autonomous actin-binding protein
    • Grubinger, M., and M. Gimona. 2004. CRP2 is an autonomous actin-binding protein. FEBS Lett. 557:88-92.
    • (2004) FEBS Lett. , vol.557 , pp. 88-92
    • Grubinger, M.1    Gimona, M.2
  • 36
    • 44349184388 scopus 로고    scopus 로고
    • HDAC4 and PCAF bind to cardiac sarcomeres and play a role in regulating myofilament contractile activity
    • Gupta, M. P., S. A. Samant, S. H. Smith, and S. G. Shroff. 2008. HDAC4 and PCAF bind to cardiac sarcomeres and play a role in regulating myofilament contractile activity. J. Biol. Chem. 283:10135-10146.
    • (2008) J. Biol. Chem. , vol.283 , pp. 10135-10146
    • Gupta, M.P.1    Samant, S.A.2    Smith, S.H.3    Shroff, S.G.4
  • 38
    • 0027439319 scopus 로고
    • Human actin depolymerizing factor mediates a pH-sensitive destruction of actin filaments
    • Hawkins, M., B. Pope, S. K. Maciver, and A. G. Weeds. 1993. Human actin depolymerizing factor mediates a pH-sensitive destruction of actin filaments. Biochemistry 32:9985-9993.
    • (1993) Biochemistry , vol.32 , pp. 9985-9993
    • Hawkins, M.1    Pope, B.2    Maciver, S.K.3    Weeds, A.G.4
  • 39
    • 0027494863 scopus 로고
    • Analysis of the interactions of actin depolymerizing factor with G- And F- actin
    • DOI 10.1021/bi00089a015
    • Hayden, S. M., P. S. Miller, A. Brauweiler, and J. R. Bamburg. 1993. Analysis of the interactions of actin depolymerizing factor with G- and F-actin. Biochemistry 32:9994-10004. (Pubitemid 23312425)
    • (1993) Biochemistry , vol.32 , Issue.38 , pp. 9994-10004
    • Hayden, S.M.1    Miller, P.S.2    Brauweiler, A.3    Bamburg, J.R.4
  • 40
  • 41
    • 34548775860 scopus 로고    scopus 로고
    • Activity of cofilin can be regulated by a mechanism other than phosphorylation/dephosphorylation in muscle cells in culture
    • Hosoda, A., N. Sato, R. Nagaoka, H. Abe, and T. Obinata. 2007. Activity of cofilin can be regulated by a mechanism other than phosphorylation/ dephosphorylation in muscle cells in culture. J. Muscle Res. Cell Motil. 28:183-194.
    • (2007) J. Muscle Res. Cell Motil. , vol.28 , pp. 183-194
    • Hosoda, A.1    Sato, N.2    Nagaoka, R.3    Abe, H.4    Obinata, T.5
  • 42
    • 0027475652 scopus 로고
    • Isolation of a yeast essential gene, COF1, that encodes a homologue of mammalian cofilin, a low-M(r) actin-binding and depolymerizing protein
    • DOI 10.1016/0378-1119(93)90770-4
    • Iida, K., K. Moriyama, S. Matsumoto, H. Kawasaki, E. Nishida, and I. Yahara. 1993. Isolation of a yeast essential gene, COF1, that encodes a homologue of mammalian cofilin, a low-M(r) actin-binding and depolymerizing protein. Gene. 124:115-120. (Pubitemid 23065976)
    • (1993) Gene , vol.124 , Issue.1 , pp. 115-120
    • Iida, K.1    Moriyama, K.2    Matsumoto, S.3    Kawasaki, H.4    Nishida, E.5    Yahara, I.6
  • 43
    • 42749083194 scopus 로고    scopus 로고
    • The role of NHE-1 in myocardial hypertrophy and remodelling
    • Karmazyn, M., A. Kilic, and S. Javadov. 2008. The role of NHE-1 in myocardial hypertrophy and remodelling. J. Mol. Cell Cardiol. 44:647-653.
    • (2008) J. Mol. Cell Cardiol. , vol.44 , pp. 647-653
    • Karmazyn, M.1    Kilic, A.2    Javadov, S.3
  • 44
    • 0014591697 scopus 로고
    • Editorial: The early "pump" failure of the ischemic heart
    • Katz, A. M., and H. H. Hecht. 1969. Editorial: the early "pump" failure of the ischemic heart. Am. J. Med. 47:497-502.
    • (1969) Am. J. Med. , vol.47 , pp. 497-502
    • Katz, A.M.1    Hecht, H.H.2
  • 47
    • 0030753648 scopus 로고    scopus 로고
    • Muscle LIM protein promotes myogenesis by enhancing the activity of MyoD
    • Kong, Y., M. J. Flick, A. J. Kudla, and S. F. Konieczny. 1997. Muscle LIM protein promotes myogenesis by enhancing the activity of MyoD. Mol. Cell. Biol. 17:4750-4760.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 4750-4760
    • Kong, Y.1    Flick, M.J.2    Kudla, A.J.3    Konieczny, S.F.4
  • 48
    • 36849093327 scopus 로고    scopus 로고
    • Proper perinuclear localization of the TRIM-like protein myospryn requires its binding partner desmin
    • Kouloumenta, A., M. Mavroidis, and Y. Capetanaki. 2007. Proper perinuclear localization of the TRIM-like protein myospryn requires its binding partner desmin. J. Biol. Chem. 282:35211-35221.
    • (2007) J. Biol. Chem. , vol.282 , pp. 35211-35221
    • Kouloumenta, A.1    Mavroidis, M.2    Capetanaki, Y.3
  • 50
    • 0032959413 scopus 로고    scopus 로고
    • Reduced cytosolic acidification during exercise suggests defective glycolytic activity in skeletal muscle of patients with Becker muscular dystrophy. An in vivo 31P magnetic resonance spectroscopy study
    • Lodi, R., G. J. Kemp, F. Muntoni, C. H. Thompson, C. Rae, J. Taylor, P. Styles, and D. J. Taylor. 1999. Reduced cytosolic acidification during exercise suggests defective glycolytic activity in skeletal muscle of patients with Becker muscular dystrophy. An in vivo 31P magnetic resonance spectroscopy study. Brain 122:121-130.
    • (1999) Brain , vol.122 , pp. 121-130
    • Lodi, R.1    Kemp, G.J.2    Muntoni, F.3    Thompson, C.H.4    Rae, C.5    Taylor, J.6    Styles, P.7    Taylor, D.J.8
  • 51
    • 0030871066 scopus 로고    scopus 로고
    • Comparison of three members of the cysteine-rich protein family reveals functional conservation and divergent patterns of gene expression
    • Louis, H. A., J. D. Pino, K. L. Schmeichel, P. Pomies, and M. C. Beckerle. 1997. Comparison of three members of the cysteine-rich protein family reveals functional conservation and divergent patterns of gene expression. J. Biol. Chem. 272:27484-27491.
    • (1997) J. Biol. Chem. , vol.272 , pp. 27484-27491
    • Louis, H.A.1    Pino, J.D.2    Schmeichel, K.L.3    Pomies, P.4    Beckerle, M.C.5
  • 52
    • 0038464639 scopus 로고    scopus 로고
    • Phospholamban: A crucial regulator of cardiac contractility
    • MacLennan, D. H., and E. G. Kranias. 2003. Phospholamban: a crucial regulator of cardiac contractility. Nat. Rev. Mol. Cell Biol. 4:566-577.
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 566-577
    • MacLennan, D.H.1    Kranias, E.G.2
  • 54
    • 0029083650 scopus 로고
    • Prevalence of hypertrophic cardiomyopathy in a general population of young adults. Echocardiographic analysis of 4111 subjects in the CARDIA Study
    • Coronary Artery Risk Development in (Young) Adults
    • Maron, B. J., J. M. Gardin, J. M. Flack, S. S. Gidding, T. T. Kurosaki, and D. E. Bild. 1995. Prevalence of hypertrophic cardiomyopathy in a general population of young adults. Echocardiographic analysis of 4111 subjects in the CARDIA Study. Coronary Artery Risk Development in (Young) Adults. Circulation 92:785-789.
    • (1995) Circulation , vol.92 , pp. 785-789
    • Maron, B.J.1    Gardin, J.M.2    Flack, J.M.3    Gidding, S.S.4    Kurosaki, T.T.5    Bild, D.E.6
  • 56
    • 0029886381 scopus 로고    scopus 로고
    • Chronic muscle stimulation increases lactate transport in rat skeletal muscle
    • McCullagh, K. J., C. Juel, M. O'Brien, and A. Bonen. 1996. Chronic muscle stimulation increases lactate transport in rat skeletal muscle. Mol. Cell Biochem. 156:51-57.
    • (1996) Mol. Cell Biochem. , vol.156 , pp. 51-57
    • McCullagh, K.J.1    Juel, C.2    O'Brien, M.3    Bonen, A.4
  • 57
    • 0030820734 scopus 로고    scopus 로고
    • Cofilin changes the twist of F-actin: Implications for actin filament dynamics and cellular function
    • McGough, A., B. Pope, W. Chiu, and A. Weeds. 1997. Cofilin changes the twist of F-actin: implications for actin filament dynamics and cellular function. J. Cell Biol. 138:771-781.
    • (1997) J. Cell Biol. , vol.138 , pp. 771-781
    • McGough, A.1    Pope, B.2    Chiu, W.3    Weeds, A.4
  • 58
    • 0031952055 scopus 로고    scopus 로고
    • Actin depolymerizing factor and cofilin phosphorylation dynamics: Response to signals that regulate neurite extension
    • Meberg, P. J., S. Ono, L. S. Minamide, M. Takahashi, and J. R. Bamburg. 1998. Actin depolymerizing factor and cofilin phosphorylation dynamics: response to signals that regulate neurite extension. Cell Motil. Cytoskeleton 39:172-190.
    • (1998) Cell Motil. Cytoskeleton , vol.39 , pp. 172-190
    • Meberg, P.J.1    Ono, S.2    Minamide, L.S.3    Takahashi, M.4    Bamburg, J.R.5
  • 59
    • 0029738727 scopus 로고    scopus 로고
    • Disruption of muscle architecture and myocardial degeneration in mice lacking desmin
    • Milner, D. J., G. Weitzer, D. Tran, A. Bradley, and Y. Capetanaki. 1996. Disruption of muscle architecture and myocardial degeneration in mice lacking desmin. J. Cell Biol. 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
  • 62
    • 0029678546 scopus 로고    scopus 로고
    • Phosphorylation of Ser-3 of cofilin regulates its essential function on actin
    • Moriyama, K., K. Iida, and I. Yahara. 1996. Phosphorylation of Ser-3 of cofilin regulates its essential function on actin. Genes Cells 1:73-86. (Pubitemid 126673108)
    • (1996) Genes to Cells , vol.1 , Issue.1 , pp. 73-86
    • Moriyama, K.1    Iida, K.2    Yahara, I.3
  • 63
    • 28244484957 scopus 로고    scopus 로고
    • Two mouse cofilin isoforms, muscle-type (MCF) and non-muscle type (NMCF), interact with F-actin with different efficiencies
    • Tokyo
    • Nakashima, K., N. Sato, T. Nakagaki, H. Abe, S. Ono, and T. Obinata. 2005. Two mouse cofilin isoforms, muscle-type (MCF) and non-muscle type (NMCF), interact with F-actin with different efficiencies. J. Biochem. (Tokyo) 138:519-526.
    • (2005) J. Biochem. , vol.138 , pp. 519-526
    • Nakashima, K.1    Sato, N.2    Nakagaki, T.3    Abe, H.4    Ono, S.5    Obinata, T.6
  • 64
    • 0037169335 scopus 로고    scopus 로고
    • Control of actin reorganization by slingshot, a family of phosphatases that dephosphorylate ADF/cofilin
    • DOI 10.1016/S0092-8674(01)00638-9
    • Niwa, R., K. Nagata-Ohashi, M. Takeichi, K. Mizuno, and T. Uemura. 2002. Control of actin reorganization by Slingshot, a family of phosphatases that dephosphorylate ADF/cofilin. Cell 108:233-246. (Pubitemid 34161143)
    • (2002) Cell , vol.108 , Issue.2 , pp. 233-246
    • Niwa, R.1    Nagata-Ohashi, K.2    Takeichi, M.3    Mizuno, K.4    Uemura, T.5
  • 65
    • 0028283542 scopus 로고
    • Characterization of a novel cofilin isoform that is predominantly expressed in mammalian skeletal muscle
    • Ono, S., N. Minami, H. Abe, and T. Obinata. 1994. Characterization of a novel cofilin isoform that is predominantly expressed in mammalian skeletal muscle. J. Biol. Chem. 269:15280-15286.
    • (1994) J. Biol. Chem. , vol.269 , pp. 15280-15286
    • Ono, S.1    Minami, N.2    Abe, H.3    Obinata, T.4
  • 67
    • 0016660035 scopus 로고
    • Intracellular pH and K+ of cardiac and skeletal muscle in acidosis and alkalosis
    • Poole-Wilson, P. A., and I. R. Cameron. 1975. Intracellular pH and K+ of cardiac and skeletal muscle in acidosis and alkalosis. Am. J. Physiol. 229:1305-1310.
    • (1975) Am. J. Physiol. , vol.229 , pp. 1305-1310
    • Poole-Wilson, P.A.1    Cameron, I.R.2
  • 68
    • 1042289739 scopus 로고    scopus 로고
    • Solution structure of human cofilin: Actin binding, pH sensitivity, and relationship to actin-depolymerizing factor
    • Pope, B. J., K. M. Zierler-Gould, R. Kuhne, A. G. Weeds, and L. J. Ball. 2004. Solution structure of human cofilin: actin binding, pH sensitivity, and relationship to actin-depolymerizing factor. J. Biol. Chem. 279:4840-4848.
    • (2004) J. Biol. Chem. , vol.279 , pp. 4840-4848
    • Pope, B.J.1    Zierler-Gould, K.M.2    Kuhne, R.3    Weeds, A.G.4    Ball, L.J.5
  • 69
    • 43449130018 scopus 로고    scopus 로고
    • Zebrafish integrin-linked kinase is required in skeletal muscles for strengthening the integrin-ECM adhesion complex
    • Postel, R., P. Vakeel, J. Topczewski, R. Knoll, and J. Bakkers. 2008. Zebrafish integrin-linked kinase is required in skeletal muscles for strengthening the integrin-ECM adhesion complex. Dev. Biol. 318:92-101.
    • (2008) Dev. Biol. , vol.318 , pp. 92-101
    • Postel, R.1    Vakeel, P.2    Topczewski, J.3    Knoll, R.4    Bakkers, J.5
  • 71
    • 0034906020 scopus 로고    scopus 로고
    • Clinical and genetic heterogeneity in nemaline myopathy-a disease of skeletal muscle thin filaments
    • Sanoudou, D., and A. H. Beggs. 2001. Clinical and genetic heterogeneity in nemaline myopathy-a disease of skeletal muscle thin filaments. Trends Mol. Med. 7:362-368.
    • (2001) Trends Mol. Med. , vol.7 , pp. 362-368
    • Sanoudou, D.1    Beggs, A.H.2
  • 73
    • 0032816509 scopus 로고    scopus 로고
    • Muscle LIM proteins are associated with muscle sarcomeres and require dMEF2 for their expression during Drosophila myogenesis
    • Stronach, B. E., P. J. Renfranz, B. Lilly, and M. C. Beckerle. 1999. Muscle LIM proteins are associated with muscle sarcomeres and require dMEF2 for their expression during Drosophila myogenesis. Mol. Biol. Cell 10:2329-2342.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 2329-2342
    • Stronach, B.E.1    Renfranz, P.J.2    Lilly, B.3    Beckerle, M.C.4
  • 74
    • 0033611107 scopus 로고    scopus 로고
    • Cofilin phosphorylation and actin cytoskeletal dynamics regulated by Rho- And Cdc42-activated LIM-kinase 2
    • DOI 10.1083/jcb.147.7.1519
    • Sumi, T., K. Matsumoto, Y. Takai, and T. Nakamura. 1999. Cofilin phosphorylation and actin cytoskeletal dynamics regulated by rho- and Cdc42-activated LIM-kinase 2. J. Cell Biol. 147:1519-1532. (Pubitemid 30027406)
    • (1999) Journal of Cell Biology , vol.147 , Issue.7 , pp. 1519-1532
    • Sumi, T.1    Matsumoto, K.2    Takai, Y.3    Nakamura, T.4
  • 76
    • 33644849222 scopus 로고    scopus 로고
    • Heart disease and stroke statistics - 2006 Update: A report from the American Heart Association Statistics Committee and Stroke Statistics Subcommittee
    • DOI 10.1161/CIRCULATIONAHA.105.171600, PII 0000301720060214000028
    • Thom, T., N. Haase, W. Rosamond, V. J. Howard, J. Rumsfeld, T. Manolio, Z. J. Zheng, K. Flegal, C. O'Donnell, S. Kittner, D. Lloyd-Jones, D. C. Goff, Jr., Y. Hong, R. Adams, G. Friday, K. Furie, P. Gorelick, B. Kissela, J. Marler, J. Meigs, V. Roger, S. Sidney, P. Sorlie, J. Steinberger, S. Wasserthiel-Smoller, M. Wilson, and P. Wolf. 2006. Heart disease and stroke statistics-2006 update: a report from the American Heart Association Statistics Committee and Stroke Statistics Subcommittee. Circulation 113:e85-e151. (Pubitemid 43754289)
    • (2006) Circulation , vol.113 , Issue.6
    • Thom, T.1    Haase, N.2    Rosamond, W.3    Howard, V.J.4    Rumsfeld, J.5    Manolio, T.6    Zheng, Z.-J.7    Flegal, K.8    O'Donnell, C.9    Kittner, S.10    Lloyd-Jones, D.11    Goff Jr., D.C.12    Hong, Y.13
  • 77
    • 0035171699 scopus 로고    scopus 로고
    • Cofilin phosphorylation by protein kinase testicular protein kinase 1 and its role in integrin-mediated actin reorganization and focal adhesion formation
    • Toshima, J., J. Y. Toshima, T. Amano, N. Yang, S. Narumiya, and K. Mizuno. 2001. Cofilin phosphorylation by protein kinase testicular protein kinase 1 and its role in integrin-mediated actin reorganization and focal adhesion formation. Mol. Biol. Cell 12:1131-1145.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 1131-1145
    • Toshima, J.1    Toshima, J.Y.2    Amano, T.3    Yang, N.4    Narumiya, S.5    Mizuno, K.6
  • 78
    • 0035903099 scopus 로고    scopus 로고
    • Cofilin phosphorylation and actin reorganization activities of testicular protein kinase 2 and its predominant expression in testicular Sertoli cells
    • Toshima, J., J. Y. Toshima, K. Takeuchi, R. Mori, and K. Mizuno. 2001. Cofilin phosphorylation and actin reorganization activities of testicular protein kinase 2 and its predominant expression in testicular Sertoli cells. J. Biol. Chem. 276:31449-31458.
    • (2001) J. Biol. Chem. , vol.276 , pp. 31449-31458
    • Toshima, J.1    Toshima, J.Y.2    Takeuchi, K.3    Mori, R.4    Mizuno, K.5
  • 79
  • 80
    • 0036153765 scopus 로고    scopus 로고
    • The three mouse actin-depolymerizing factor/cofilins evolved to fulfill cell-type-specific requirements for actin dynamics
    • Vartiainen, M. K., T. Mustonen, P. K. Mattila, P. J. Ojala, I. Thesleff, J. Partanen, and P. Lappalainen. 2002. The three mouse actin-depolymerizing factor/cofilins evolved to fulfill cell-type-specific requirements for actin dynamics. Mol. Biol. Cell 13:183-194.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 183-194
    • Vartiainen, M.K.1    Mustonen, T.2    Mattila, P.K.3    Ojala, P.J.4    Thesleff, I.5    Partanen, J.6    Lappalainen, P.7
  • 82
    • 11244256463 scopus 로고    scopus 로고
    • Dystrophin- and MLP-deficient mouse hearts: Marked differences in morphology and function, but similar accumulation of cytoskeletal proteins
    • Wilding, J. R., J. E. Schneider, A. E. Sang, K. E. Davies, S. Neubauer, and K. Clarke. 2005. Dystrophin- and MLP-deficient mouse hearts: marked differences in morphology and function, but similar accumulation of cytoskeletal proteins. FASEB J. 19:79-81.
    • (2005) FASEB J. , vol.19 , pp. 79-81
    • Wilding, J.R.1    Schneider, J.E.2    Sang, A.E.3    Davies, K.E.4    Neubauer, S.5    Clarke, K.6
  • 85
    • 0032565769 scopus 로고    scopus 로고
    • Cofflin phosphorylation by LIM-kinase 1 and its role in Rac-mediated actin reorganization
    • DOI 10.1038/31735
    • Yang, N., O. Higuchi, K. Ohashi, K. Nagata, A. Wada, K. Kangawa, E. Nishida, and K. Mizuno. 1998. Cofilin phosphorylation by LIM-kinase 1 and its role in Rac-mediated actin reorganization. Nature 393:809-812. (Pubitemid 28299495)
    • (1998) Nature , vol.393 , Issue.6687 , pp. 809-812
    • Yang, N.1    Higuchi, O.2    Ohashi, K.3    Nagata, K.4    Wada, A.5    Kangawa, K.6    Nishida, E.7    Mizuno, K.8
  • 86
    • 0036304481 scopus 로고    scopus 로고
    • Determining the differences in actin binding by human ADF and cofilin
    • Yeoh, S., B. Pope, H. G. Mannherz, and A. Weeds. 2002. Determining the differences in actin binding by human ADF and cofilin. J. Mol. Biol. 315:911-925.
    • (2002) J. Mol. Biol. , vol.315 , pp. 911-925
    • Yeoh, S.1    Pope, B.2    Mannherz, H.G.3    Weeds, A.4
  • 87
    • 0022403777 scopus 로고
    • pH control of actin polymerization by cofilin
    • Yonezawa, N., E. Nishida, and H. Sakai. 1985. pH control of actin polymerization by cofilin. J. Biol. Chem. 260:14410-14412.
    • (1985) J. Biol. Chem. , vol.260 , pp. 14410-14412
    • Yonezawa, N.1    Nishida, E.2    Sakai, H.3
  • 88
    • 12244262321 scopus 로고    scopus 로고
    • Products of phosphoinositide specific phospholipase C can trigger dephosphorylation of cofilin in chemoattractant stimulated neutrophils
    • DOI 10.1002/cm.10079
    • Zhan, Q., J. R. Bamburg, and J. A. Badwey. 2003. Products of phosphoinositide specific phospholipase C can trigger dephosphorylation of cofilin in chemoattractant stimulated neutrophils. Cell Motil. Cytoskeleton 54:1-15. (Pubitemid 36033834)
    • (2003) Cell Motility and the Cytoskeleton , vol.54 , Issue.1 , pp. 1-15
    • Zhan, Q.1    Bamburg, J.R.2    Badwey, J.A.3
  • 89
    • 0034643946 scopus 로고    scopus 로고
    • Decreased expression of the cardiac LIM domain protein MLP in chronic human heart failure
    • Zolk, O., P. Caroni, and M. Bohm. 2000. Decreased expression of the cardiac LIM domain protein MLP in chronic human heart failure. Circulation 101:2674-2677. (Pubitemid 30390568)
    • (2000) Circulation , vol.101 , Issue.23 , pp. 2674-2677
    • Zolk, O.1    Caroni, P.2    Bohm, M.3


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