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Volumn 31, Issue 2, 2014, Pages 215-226

Cofilin-2 controls actin filament length in muscle sarcomeres

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; ALPHA ACTIN; COFILIN 1; COFILIN 2; F ACTIN; TROPOMODULIN; ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; ADP-G-ACTIN; ATP-G-ACTIN; PROTEIN BINDING; SMALL INTERFERING RNA;

EID: 84908466763     PISSN: 15345807     EISSN: 18781551     Source Type: Journal    
DOI: 10.1016/j.devcel.2014.09.002     Document Type: Article
Times cited : (68)

References (67)
  • 1
    • 24344470264 scopus 로고    scopus 로고
    • The M-band: an elastic web that crosslinks thick filaments in the center of the sarcomere
    • Agarkova I., Perriard J.-C. The M-band: an elastic web that crosslinks thick filaments in the center of the sarcomere. Trends Cell Biol. 2005, 15:477-485.
    • (2005) Trends Cell Biol. , vol.15 , pp. 477-485
    • Agarkova, I.1    Perriard, J.-C.2
  • 3
    • 84860466060 scopus 로고    scopus 로고
    • Normal myofibrillar development followed by progressive sarcomeric disruption with actin accumulations in a mouse Cfl2 knockout demonstrates requirement of cofilin-2 for muscle maintenance
    • Agrawal P.B., Joshi M., Savic T., Chen Z., Beggs A.H. Normal myofibrillar development followed by progressive sarcomeric disruption with actin accumulations in a mouse Cfl2 knockout demonstrates requirement of cofilin-2 for muscle maintenance. Hum. Mol. Genet. 2012, 21:2341-2356.
    • (2012) Hum. Mol. Genet. , vol.21 , pp. 2341-2356
    • Agrawal, P.B.1    Joshi, M.2    Savic, T.3    Chen, Z.4    Beggs, A.H.5
  • 4
    • 33749046492 scopus 로고    scopus 로고
    • Mechanism of actin filament turnover by severing and nucleation at different concentrations of ADF/cofilin
    • Andrianantoandro E., Pollard T.D. Mechanism of actin filament turnover by severing and nucleation at different concentrations of ADF/cofilin. Mol. Cell 2006, 24:13-23.
    • (2006) Mol. Cell , vol.24 , pp. 13-23
    • Andrianantoandro, E.1    Pollard, T.D.2
  • 5
    • 34548850904 scopus 로고    scopus 로고
    • N-cofilin is associated with neuronal migration disorders and cell cycle control in the cerebral cortex
    • Bellenchi G.C., Gurniak C.B., Perlas E., Middei S., Ammassari-Teule M., Witke W. N-cofilin is associated with neuronal migration disorders and cell cycle control in the cerebral cortex. Genes Dev. 2007, 21:2347-2357.
    • (2007) Genes Dev. , vol.21 , pp. 2347-2357
    • Bellenchi, G.C.1    Gurniak, C.B.2    Perlas, E.3    Middei, S.4    Ammassari-Teule, M.5    Witke, W.6
  • 6
    • 77950859278 scopus 로고    scopus 로고
    • ADF/cofilin: a functional node in cell biology
    • Bernstein B.W., Bamburg J.R. ADF/cofilin: a functional node in cell biology. Trends Cell Biol. 2010, 20:187-195.
    • (2010) Trends Cell Biol. , vol.20 , pp. 187-195
    • Bernstein, B.W.1    Bamburg, J.R.2
  • 7
    • 2342514815 scopus 로고    scopus 로고
    • Cyclase-associated protein 1 (CAP1) promotes cofilin-induced actin dynamics in mammalian nonmuscle cells
    • Bertling E., Hotulainen P., Mattila P.K., Matilainen T., Salminen M., Lappalainen P. Cyclase-associated protein 1 (CAP1) promotes cofilin-induced actin dynamics in mammalian nonmuscle cells. Mol. Biol. Cell 2004, 15:2324-2334.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 2324-2334
    • Bertling, E.1    Hotulainen, P.2    Mattila, P.K.3    Matilainen, T.4    Salminen, M.5    Lappalainen, P.6
  • 8
    • 77952896939 scopus 로고    scopus 로고
    • Control of actin filament treadmilling in cell motility
    • Bugyi B., Carlier M.-F. Control of actin filament treadmilling in cell motility. Annu. Rev. Biophys. 2010, 39:449-470.
    • (2010) Annu. Rev. Biophys. , vol.39 , pp. 449-470
    • Bugyi, B.1    Carlier, M.-F.2
  • 9
    • 0030843484 scopus 로고    scopus 로고
    • Actin depolymerizing factor (ADF/cofilin) enhances the rate of filament turnover: implication in actin-based motility
    • Carlier M.F., Laurent V., Santolini J., Melki R., Didry D., Xia G.X., Hong Y., Chua N.H., Pantaloni D. Actin depolymerizing factor (ADF/cofilin) enhances the rate of filament turnover: implication in actin-based motility. J.Cell Biol. 1997, 136:1307-1322.
    • (1997) J.Cell Biol. , vol.136 , pp. 1307-1322
    • Carlier, M.F.1    Laurent, V.2    Santolini, J.3    Melki, R.4    Didry, D.5    Xia, G.X.6    Hong, Y.7    Chua, N.H.8    Pantaloni, D.9
  • 11
    • 0024297288 scopus 로고
    • Probing the mechanism of ATP hydrolysis on F-actin using vanadate and the structural analogs of phosphate BeF-3 and A1F-4
    • Combeau C., Carlier M.F. Probing the mechanism of ATP hydrolysis on F-actin using vanadate and the structural analogs of phosphate BeF-3 and A1F-4. J.Biol. Chem. 1988, 263:17429-17436.
    • (1988) J.Biol. Chem. , vol.263 , pp. 17429-17436
    • Combeau, C.1    Carlier, M.F.2
  • 12
    • 48949106158 scopus 로고    scopus 로고
    • New insights into mechanism and regulation of actin capping protein
    • Cooper J.A., Sept D. New insights into mechanism and regulation of actin capping protein. Int. Rev. Cell. Mol. Biol. 2008, 267:183-206.
    • (2008) Int. Rev. Cell. Mol. Biol. , vol.267 , pp. 183-206
    • Cooper, J.A.1    Sept, D.2
  • 13
    • 0019853076 scopus 로고
    • 7-Chloro-4-nitrobenzeno-2-oxa-1,3-diazole actin as a probe for actin polymerization
    • Detmers P., Weber A., Elzinga M., Stephens R.E. 7-Chloro-4-nitrobenzeno-2-oxa-1,3-diazole actin as a probe for actin polymerization. J.Biol. Chem. 1981, 256:99-105.
    • (1981) J.Biol. Chem. , vol.256 , pp. 99-105
    • Detmers, P.1    Weber, A.2    Elzinga, M.3    Stephens, R.E.4
  • 14
    • 6344228185 scopus 로고    scopus 로고
    • Actin-binding proteins-a unifying hypothesis
    • Dominguez R. Actin-binding proteins-a unifying hypothesis. Trends Biochem. Sci. 2004, 29:572-578.
    • (2004) Trends Biochem. Sci. , vol.29 , pp. 572-578
    • Dominguez, R.1
  • 16
    • 84876041581 scopus 로고    scopus 로고
    • Biophysics of actin filament severing by cofilin
    • Elam W.A., Kang H., De la Cruz E.M. Biophysics of actin filament severing by cofilin. FEBS Lett. 2013, 587:1215-1219.
    • (2013) FEBS Lett. , vol.587 , pp. 1215-1219
    • Elam, W.A.1    Kang, H.2    De la Cruz, E.M.3
  • 17
    • 77957996302 scopus 로고    scopus 로고
    • Direct visualization of secondary structures of F-actin by electron cryomicroscopy
    • Fujii T., Iwane A.H., Yanagida T., Namba K. Direct visualization of secondary structures of F-actin by electron cryomicroscopy. Nature 2010, 467:724-728.
    • (2010) Nature , vol.467 , pp. 724-728
    • Fujii, T.1    Iwane, A.H.2    Yanagida, T.3    Namba, K.4
  • 18
    • 34547455419 scopus 로고    scopus 로고
    • Polymerization kinetics of ADP- and ADP-Pi-actin determined by fluorescence microscopy
    • Fujiwara I., Vavylonis D., Pollard T.D. Polymerization kinetics of ADP- and ADP-Pi-actin determined by fluorescence microscopy. Proc. Natl. Acad. Sci. USA 2007, 104:8827-8832.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 8827-8832
    • Fujiwara, I.1    Vavylonis, D.2    Pollard, T.D.3
  • 20
    • 65549103882 scopus 로고    scopus 로고
    • Coronin switches roles in actin disassembly depending on the nucleotide state of actin
    • Gandhi M., Achard V., Blanchoin L., Goode B.L. Coronin switches roles in actin disassembly depending on the nucleotide state of actin. Mol. Cell 2009, 34:364-374.
    • (2009) Mol. Cell , vol.34 , pp. 364-374
    • Gandhi, M.1    Achard, V.2    Blanchoin, L.3    Goode, B.L.4
  • 21
    • 84872925287 scopus 로고    scopus 로고
    • A two-segment model for thin filament architecture in skeletal muscle
    • Gokhin D.S., Fowler V.M. A two-segment model for thin filament architecture in skeletal muscle. Nat. Rev. Mol. Cell Biol. 2013, 14:113-119.
    • (2013) Nat. Rev. Mol. Cell Biol. , vol.14 , pp. 113-119
    • Gokhin, D.S.1    Fowler, V.M.2
  • 22
    • 11844276055 scopus 로고    scopus 로고
    • The actin depolymerizing factor n-cofilin is essential for neural tube morphogenesis and neural crest cell migration
    • Gurniak C.B., Perlas E., Witke W. The actin depolymerizing factor n-cofilin is essential for neural tube morphogenesis and neural crest cell migration. Dev. Biol. 2005, 278:231-241.
    • (2005) Dev. Biol. , vol.278 , pp. 231-241
    • Gurniak, C.B.1    Perlas, E.2    Witke, W.3
  • 24
    • 0027439319 scopus 로고
    • Human actin depolymerizing factor mediates a pH-sensitive destruction of actin filaments
    • Hawkins M., Pope B., Maciver S.K., Weeds A.G. Human actin depolymerizing factor mediates a pH-sensitive destruction of actin filaments. Biochemistry 1993, 32:9985-9993.
    • (1993) Biochemistry , vol.32 , pp. 9985-9993
    • Hawkins, M.1    Pope, B.2    Maciver, S.K.3    Weeds, A.G.4
  • 25
    • 0027494863 scopus 로고
    • Analysis of the interactions of actin depolymerizing factor with G- and F-actin
    • Hayden S.M., Miller P.S., Brauweiler A., Bamburg J.R. Analysis of the interactions of actin depolymerizing factor with G- and F-actin. Biochemistry 1993, 32:9994-10004.
    • (1993) Biochemistry , vol.32 , pp. 9994-10004
    • Hayden, S.M.1    Miller, P.S.2    Brauweiler, A.3    Bamburg, J.R.4
  • 26
    • 85012414651 scopus 로고
    • Electron microscope studies on the structure of natural and synthetic protein filaments from striated muscle
    • Huxley H.E. Electron microscope studies on the structure of natural and synthetic protein filaments from striated muscle. J.Mol. Biol. 1963, 7:281-308.
    • (1963) J.Mol. Biol. , vol.7 , pp. 281-308
    • Huxley, H.E.1
  • 27
    • 0037688016 scopus 로고    scopus 로고
    • Aberrant actin cytoskeleton leads to accelerated proliferation of corneal epithelial cells in mice deficient for destrin (actin depolymerizing factor)
    • Ikeda S., Cunningham L.A., Boggess D., Hawes N., Hobson C.D., Sundberg J.P., Naggert J.K., Smith R.S., Nishina P.M. Aberrant actin cytoskeleton leads to accelerated proliferation of corneal epithelial cells in mice deficient for destrin (actin depolymerizing factor). Hum. Mol. Genet. 2003, 12:1029-1037.
    • (2003) Hum. Mol. Genet. , vol.12 , pp. 1029-1037
    • Ikeda, S.1    Cunningham, L.A.2    Boggess, D.3    Hawes, N.4    Hobson, C.D.5    Sundberg, J.P.6    Naggert, J.K.7    Smith, R.S.8    Nishina, P.M.9
  • 28
    • 78650078032 scopus 로고    scopus 로고
    • Formin follows function: a muscle-specific isoform of FHOD3 is regulated by CK2 phosphorylation and promotes myofibril maintenance
    • Iskratsch T., Lange S., Dwyer J., Kho A.L., dos Remedios C., Ehler E. Formin follows function: a muscle-specific isoform of FHOD3 is regulated by CK2 phosphorylation and promotes myofibril maintenance. J.Cell Biol. 2010, 191:1159-1172.
    • (2010) J.Cell Biol. , vol.191 , pp. 1159-1172
    • Iskratsch, T.1    Lange, S.2    Dwyer, J.3    Kho, A.L.4    dos Remedios, C.5    Ehler, E.6
  • 29
    • 84862303485 scopus 로고    scopus 로고
    • The sarcomeric cytoskeleton as a target for pharmacological intervention
    • Kho A.L., Perera S., Alexandrovich A., Gautel M. The sarcomeric cytoskeleton as a target for pharmacological intervention. Curr. Opin. Pharmacol. 2012, 12:347-354.
    • (2012) Curr. Opin. Pharmacol. , vol.12 , pp. 347-354
    • Kho, A.L.1    Perera, S.2    Alexandrovich, A.3    Gautel, M.4
  • 30
    • 0028824480 scopus 로고
    • Titins: giant proteins in charge of muscle ultrastructure and elasticity
    • Labeit S., Kolmerer B. Titins: giant proteins in charge of muscle ultrastructure and elasticity. Science 1995, 270:293-296.
    • (1995) Science , vol.270 , pp. 293-296
    • Labeit, S.1    Kolmerer, B.2
  • 31
    • 30444458378 scopus 로고    scopus 로고
    • From A to Z and back? Multicompartment proteins in the sarcomere
    • Lange S., Ehler E., Gautel M. From A to Z and back? Multicompartment proteins in the sarcomere. Trends Cell Biol. 2006, 16:11-18.
    • (2006) Trends Cell Biol. , vol.16 , pp. 11-18
    • Lange, S.1    Ehler, E.2    Gautel, M.3
  • 32
    • 0021141093 scopus 로고
    • Brevin and vitamin D binding protein: comparison of the effects of two serum proteins on actin assembly and disassembly
    • Lees A., Haddad J.G., Lin S. Brevin and vitamin D binding protein: comparison of the effects of two serum proteins on actin assembly and disassembly. Biochemistry 1984, 23:3038-3047.
    • (1984) Biochemistry , vol.23 , pp. 3038-3047
    • Lees, A.1    Haddad, J.G.2    Lin, S.3
  • 33
    • 54549121277 scopus 로고    scopus 로고
    • Thin filament length regulation in striated muscle sarcomeres: pointed-end dynamics go beyond a nebulin ruler
    • Littlefield R.S., Fowler V.M. Thin filament length regulation in striated muscle sarcomeres: pointed-end dynamics go beyond a nebulin ruler. Semin. Cell Dev. Biol. 2008, 19:511-519.
    • (2008) Semin. Cell Dev. Biol. , vol.19 , pp. 511-519
    • Littlefield, R.S.1    Fowler, V.M.2
  • 34
    • 0034976418 scopus 로고    scopus 로고
    • Actin dynamics at pointed ends regulates thin filament length in striated muscle
    • Littlefield R., Almenar-Queralt A., Fowler V.M. Actin dynamics at pointed ends regulates thin filament length in striated muscle. Nat. Cell Biol. 2001, 3:544-551.
    • (2001) Nat. Cell Biol. , vol.3 , pp. 544-551
    • Littlefield, R.1    Almenar-Queralt, A.2    Fowler, V.M.3
  • 35
    • 84872278687 scopus 로고    scopus 로고
    • Mammalian and malaria parasite cyclase-associated proteins catalyze nucleotide exchange on G-actin through a conserved mechanism
    • Makkonen M., Bertling E., Chebotareva N.A., Baum J., Lappalainen P. Mammalian and malaria parasite cyclase-associated proteins catalyze nucleotide exchange on G-actin through a conserved mechanism. J.Biol. Chem. 2013, 288:984-994.
    • (2013) J.Biol. Chem. , vol.288 , pp. 984-994
    • Makkonen, M.1    Bertling, E.2    Chebotareva, N.A.3    Baum, J.4    Lappalainen, P.5
  • 37
    • 0030820734 scopus 로고    scopus 로고
    • Cofilin changes the twist of F-actin: implications for actin filament dynamics and cellular function
    • McGough A., Pope B., Chiu W., Weeds A. Cofilin changes the twist of F-actin: implications for actin filament dynamics and cellular function. J.Cell Biol. 1997, 138:771-781.
    • (1997) J.Cell Biol. , vol.138 , pp. 771-781
    • McGough, A.1    Pope, B.2    Chiu, W.3    Weeds, A.4
  • 39
    • 0037093266 scopus 로고    scopus 로고
    • Human CAP1 is a key factor in the recycling of cofilin and actin for rapid actin turnover
    • Moriyama K., Yahara I. Human CAP1 is a key factor in the recycling of cofilin and actin for rapid actin turnover. J.Cell Sci. 2002, 115:1591-1601.
    • (2002) J.Cell Sci. , vol.115 , pp. 1591-1601
    • Moriyama, K.1    Yahara, I.2
  • 40
    • 33845414566 scopus 로고    scopus 로고
    • Antagonistic effects of cofilin, beryllium fluoride complex, and phalloidin on subdomain 2 and nucleotide-binding cleft in F-actin
    • Muhlrad A., Ringel I., Pavlov D., Peyser Y.M., Reisler E. Antagonistic effects of cofilin, beryllium fluoride complex, and phalloidin on subdomain 2 and nucleotide-binding cleft in F-actin. Biophys. J. 2006, 91:4490-4499.
    • (2006) Biophys. J. , vol.91 , pp. 4490-4499
    • Muhlrad, A.1    Ringel, I.2    Pavlov, D.3    Peyser, Y.M.4    Reisler, E.5
  • 41
    • 28244484957 scopus 로고    scopus 로고
    • Two mouse cofilin isoforms, muscle-type (MCF) and non-muscle type (NMCF), interact with F-actin with different efficiencies
    • Nakashima K., Sato N., Nakagaki T., Abe H., Ono S., Obinata T. Two mouse cofilin isoforms, muscle-type (MCF) and non-muscle type (NMCF), interact with F-actin with different efficiencies. J.Biochem. 2005, 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
  • 42
    • 58249091719 scopus 로고    scopus 로고
    • Two biochemically distinct and tissue-specific twinfilin isoforms are generated from the mouse Twf2 gene by alternative promoter usage
    • Nevalainen E.M., Skwarek-Maruszewska A., Braun A., Moser M., Lappalainen P. Two biochemically distinct and tissue-specific twinfilin isoforms are generated from the mouse Twf2 gene by alternative promoter usage. Biochem. J. 2009, 417:593-600.
    • (2009) Biochem. J. , vol.417 , pp. 593-600
    • Nevalainen, E.M.1    Skwarek-Maruszewska, A.2    Braun, A.3    Moser, M.4    Lappalainen, P.5
  • 44
    • 58749091822 scopus 로고    scopus 로고
    • The nature of the globular- to fibrous-actin transition
    • Oda T., Iwasa M., Aihara T., Maéda Y., Narita A. The nature of the globular- to fibrous-actin transition. Nature 2009, 457:441-445.
    • (2009) Nature , vol.457 , pp. 441-445
    • Oda, T.1    Iwasa, M.2    Aihara, T.3    Maéda, Y.4    Narita, A.5
  • 45
    • 77958521897 scopus 로고    scopus 로고
    • Dynamic regulation of sarcomeric actin filaments in striated muscle
    • Ono S. Dynamic regulation of sarcomeric actin filaments in striated muscle. Cytoskeleton (Hoboken) 2010, 67:677-692.
    • (2010) Cytoskeleton (Hoboken) , vol.67 , pp. 677-692
    • Ono, S.1
  • 46
    • 0028283542 scopus 로고
    • Characterization of a novel cofilin isoform that is predominantly expressed in mammalian skeletal muscle
    • Ono S., Minami N., Abe H., Obinata T. Characterization of a novel cofilin isoform that is predominantly expressed in mammalian skeletal muscle. J.Biol. Chem. 1994, 269:15280-15286.
    • (1994) J.Biol. Chem. , vol.269 , pp. 15280-15286
    • Ono, S.1    Minami, N.2    Abe, H.3    Obinata, T.4
  • 47
    • 0037900004 scopus 로고    scopus 로고
    • Specific requirement for two ADF/cofilin isoforms in distinct actin-dependent processes in Caenorhabditis elegans
    • Ono K., Parast M., Alberico C., Benian G.M., Ono S. Specific requirement for two ADF/cofilin isoforms in distinct actin-dependent processes in Caenorhabditis elegans. J.Cell Sci. 2003, 116:2073-2085.
    • (2003) J.Cell Sci. , vol.116 , pp. 2073-2085
    • Ono, K.1    Parast, M.2    Alberico, C.3    Benian, G.M.4    Ono, S.5
  • 48
    • 0035958757 scopus 로고    scopus 로고
    • The crystal structure of uncomplexed actin in the ADP state
    • Otterbein L.R., Graceffa P., Dominguez R. The crystal structure of uncomplexed actin in the ADP state. Science 2001, 293:708-711.
    • (2001) Science , vol.293 , pp. 708-711
    • Otterbein, L.R.1    Graceffa, P.2    Dominguez, R.3
  • 49
    • 0037062405 scopus 로고    scopus 로고
    • Crystal structures of the vitamin D-binding protein and its complex with actin: structural basis of the actin-scavenger system
    • Otterbein L.R., Cosio C., Graceffa P., Dominguez R. Crystal structures of the vitamin D-binding protein and its complex with actin: structural basis of the actin-scavenger system. Proc. Natl. Acad. Sci. USA 2002, 99:8003-8008.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 8003-8008
    • Otterbein, L.R.1    Cosio, C.2    Graceffa, P.3    Dominguez, R.4
  • 50
    • 47549090623 scopus 로고    scopus 로고
    • Structure of the actin-depolymerizing factor homology domain in complex with actin
    • Paavilainen V.O., Oksanen E., Goldman A., Lappalainen P. Structure of the actin-depolymerizing factor homology domain in complex with actin. J.Cell Biol. 2008, 182:51-59.
    • (2008) J.Cell Biol. , vol.182 , pp. 51-59
    • Paavilainen, V.O.1    Oksanen, E.2    Goldman, A.3    Lappalainen, P.4
  • 51
    • 77953141955 scopus 로고    scopus 로고
    • Nebulin regulates actin filament lengths by a stabilization mechanism
    • Pappas C.T., Krieg P.A., Gregorio C.C. Nebulin regulates actin filament lengths by a stabilization mechanism. J.Cell Biol. 2010, 189:859-870.
    • (2010) J.Cell Biol. , vol.189 , pp. 859-870
    • Pappas, C.T.1    Krieg, P.A.2    Gregorio, C.C.3
  • 53
    • 34247644614 scopus 로고    scopus 로고
    • Regulation of actin filament assembly by Arp2/3 complex and formins
    • Pollard T.D. Regulation of actin filament assembly by Arp2/3 complex and formins. Annu. Rev. Biophys. Biomol. Struct. 2007, 36:451-477.
    • (2007) Annu. Rev. Biophys. Biomol. Struct. , vol.36 , pp. 451-477
    • Pollard, T.D.1
  • 54
    • 70849098888 scopus 로고    scopus 로고
    • Actin, a central player in cell shape and movement
    • Pollard T.D., Cooper J.A. Actin, a central player in cell shape and movement. Science 2009, 326:1208-1212.
    • (2009) Science , vol.326 , pp. 1208-1212
    • Pollard, T.D.1    Cooper, J.A.2
  • 55
    • 1042289739 scopus 로고    scopus 로고
    • Solution structure of human cofilin: actin binding, pH sensitivity, and relationship to actin-depolymerizing factor
    • Pope B.J., Zierler-Gould K.M., Kühne R., Weeds A.G., Ball L.J. Solution structure of human cofilin: actin binding, pH sensitivity, and relationship to actin-depolymerizing factor. J.Biol. Chem. 2004, 279:4840-4848.
    • (2004) J.Biol. Chem. , vol.279 , pp. 4840-4848
    • Pope, B.J.1    Zierler-Gould, K.M.2    Kühne, R.3    Weeds, A.G.4    Ball, L.J.5
  • 56
    • 80052990415 scopus 로고    scopus 로고
    • Actin-depolymerizing factor homology domain: a conserved fold performing diverse roles in cytoskeletal dynamics
    • Poukkula M., Kremneva E., Serlachius M., Lappalainen P. Actin-depolymerizing factor homology domain: a conserved fold performing diverse roles in cytoskeletal dynamics. Cytoskeleton (Hoboken) 2011, 68:471-490.
    • (2011) Cytoskeleton (Hoboken) , vol.68 , pp. 471-490
    • Poukkula, M.1    Kremneva, E.2    Serlachius, M.3    Lappalainen, P.4
  • 57
    • 53749089626 scopus 로고    scopus 로고
    • The dynamic Z bands of striated muscle cells
    • Sanger J.M., Sanger J.W. The dynamic Z bands of striated muscle cells. Sci. Signal. 2008, 1:pe37.
    • (2008) Sci. Signal. , vol.1 , pp. pe37
    • Sanger, J.M.1    Sanger, J.W.2
  • 60
    • 0015218407 scopus 로고
    • The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin
    • Spudich J.A., Watt S. The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin. J.Biol. Chem. 1971, 246:4866-4871.
    • (1971) J.Biol. Chem. , vol.246 , pp. 4866-4871
    • Spudich, J.A.1    Watt, S.2
  • 63
    • 0033976663 scopus 로고    scopus 로고
    • Mouse A6/twinfilin is an actin monomer-binding protein that localizes to the regions of rapid actin dynamics
    • Vartiainen M., Ojala P.J., Auvinen P., Peränen J., Lappalainen P. Mouse A6/twinfilin is an actin monomer-binding protein that localizes to the regions of rapid actin dynamics. Mol. Cell. Biol. 2000, 20:1772-1783.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 1772-1783
    • Vartiainen, M.1    Ojala, P.J.2    Auvinen, P.3    Peränen, J.4    Lappalainen, P.5
  • 64
    • 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., Mustonen T., Mattila P.K., Ojala P.J., Thesleff I., Partanen J., Lappalainen P. The three mouse actin-depolymerizing factor/cofilins evolved to fulfill cell-type-specific requirements for actin dynamics. Mol. Biol. Cell 2002, 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
  • 66
    • 27444441098 scopus 로고    scopus 로고
    • The two Caenorhabditis elegans actin-depolymerizing factor/cofilin proteins differently enhance actin filament severing and depolymerization
    • Yamashiro S., Mohri K., Ono S. The two Caenorhabditis elegans actin-depolymerizing factor/cofilin proteins differently enhance actin filament severing and depolymerization. Biochemistry 2005, 44:14238-14247.
    • (2005) Biochemistry , vol.44 , pp. 14238-14247
    • Yamashiro, S.1    Mohri, K.2    Ono, S.3
  • 67
    • 85027946629 scopus 로고    scopus 로고
    • Tropomodulins: pointed-end capping proteins that regulate actin filament architecture in diverse cell types
    • Yamashiro S., Gokhin D.S., Kimura S., Nowak R.B., Fowler V.M. Tropomodulins: pointed-end capping proteins that regulate actin filament architecture in diverse cell types. Cytoskeleton (Hoboken) 2012, 69:337-370.
    • (2012) Cytoskeleton (Hoboken) , vol.69 , pp. 337-370
    • Yamashiro, S.1    Gokhin, D.S.2    Kimura, S.3    Nowak, R.B.4    Fowler, V.M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.