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Volumn 65, Issue 12, 2015, Pages 1199-1214

Cofilin-2 phosphorylation and sequestration in myocardial aggregates: Novel pathogenetic mechanisms for idiopathic dilated cardiomyopathy

Author keywords

adenovirus; heart failure; nemaline

Indexed keywords

COFILIN 2;

EID: 84925358628     PISSN: 07351097     EISSN: 15583597     Source Type: Journal    
DOI: 10.1016/j.jacc.2015.01.031     Document Type: Article
Times cited : (60)

References (37)
  • 1
    • 84904553187 scopus 로고    scopus 로고
    • The MOGE(S) classification of cardiomyopathy for clinicians
    • E. Arbustini, N. Narula, and L. Tavazzi The MOGE(S) classification of cardiomyopathy for clinicians J Am Coll Cardiol 64 2014 304 318
    • (2014) J Am Coll Cardiol , vol.64 , pp. 304-318
    • Arbustini, E.1    Narula, N.2    Tavazzi, L.3
  • 2
    • 77950467036 scopus 로고    scopus 로고
    • Protein aggregates and novel presenilin gene variants in idiopathic dilated cardiomyopathy
    • D. Gianni, A. Li, and G. Tesco Protein aggregates and novel presenilin gene variants in idiopathic dilated cardiomyopathy Circulation 121 2010 1216 1226
    • (2010) Circulation , vol.121 , pp. 1216-1226
    • Gianni, D.1    Li, A.2    Tesco, G.3
  • 3
    • 3042711961 scopus 로고    scopus 로고
    • Desmin-related cardiomyopathy in transgenic mice: A cardiac amyloidosis
    • A. Sanbe, H. Osinska, and J.E. Saffitz Desmin-related cardiomyopathy in transgenic mice: a cardiac amyloidosis Proc Natl Acad Sci U S A 101 2004 10132 10136
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 10132-10136
    • Sanbe, A.1    Osinska, H.2    Saffitz, J.E.3
  • 4
    • 84876076016 scopus 로고    scopus 로고
    • Aging and the aggregating proteome
    • D.C. David Aging and the aggregating proteome Front Genet 3 2012 247
    • (2012) Front Genet , vol.3 , pp. 247
    • David, D.C.1
  • 5
    • 67349217063 scopus 로고    scopus 로고
    • ER and aging-protein folding and the ER stress response
    • N. Naidoo ER and aging-protein folding and the ER stress response Ageing Res Rev 8 2009 150 159
    • (2009) Ageing Res Rev , vol.8 , pp. 150-159
    • Naidoo, N.1
  • 6
    • 0000293742 scopus 로고
    • A new disease of the cortex
    • A. Alzheimer A new disease of the cortex Allg Z Psych 64 1907 146 148
    • (1907) Allg Z Psych , vol.64 , pp. 146-148
    • Alzheimer, A.1
  • 7
    • 0015261446 scopus 로고
    • The purification of amyloid fibril proteins
    • G.G. Glenner, M. Harada, and C. Isersky The purification of amyloid fibril proteins Prep Biochem 2 1972 39 51
    • (1972) Prep Biochem , vol.2 , pp. 39-51
    • Glenner, G.G.1    Harada, M.2    Isersky, C.3
  • 8
    • 0033280237 scopus 로고    scopus 로고
    • Proteins of the ADF/cofilin family: Essential regulators of actin dynamics
    • J.R. Bamburg Proteins of the ADF/cofilin family: essential regulators of actin dynamics Annu Rev Cell Dev Biol 15 1999 185 230
    • (1999) Annu Rev Cell Dev Biol , vol.15 , pp. 185-230
    • Bamburg, J.R.1
  • 9
    • 0034282106 scopus 로고    scopus 로고
    • Neurodegenerative stimuli induce persistent ADF/cofilin-actin rods that disrupt distal neurite function
    • L.S. Minamide, A.M. Striegl, J.A. Boyle, P.J. Meberg, and J.R. Bamburg Neurodegenerative stimuli induce persistent ADF/cofilin-actin rods that disrupt distal neurite function Nat Cell Biol 2 2000 628 636
    • (2000) Nat Cell Biol , vol.2 , pp. 628-636
    • Minamide, L.S.1    Striegl, A.M.2    Boyle, J.A.3    Meberg, P.J.4    Bamburg, J.R.5
  • 10
    • 78649373184 scopus 로고    scopus 로고
    • Roles of ADF/cofilin in actin polymerization and beyond
    • J.R. Bamburg, and B.W. Bernstein Roles of ADF/cofilin in actin polymerization and beyond F1000 Biol Rep 2 2010 62
    • (2010) F1000 Biol Rep , vol.2 , pp. 62
    • Bamburg, J.R.1    Bernstein, B.W.2
  • 11
    • 0036153765 scopus 로고    scopus 로고
    • The three mouse actin-depolymerizing factor/cofilins evolved to fulfill cell-type-specific requirements for actin dynamics
    • M.K. Vartiainen, T. Mustonen, and P.K. Mattila The three mouse actin-depolymerizing factor/cofilins evolved to fulfill cell-type-specific requirements for actin dynamics Mol Biol Cell 13 2002 183 194
    • (2002) Mol Biol Cell , vol.13 , pp. 183-194
    • Vartiainen, M.K.1    Mustonen, T.2    Mattila, P.K.3
  • 13
    • 33749507375 scopus 로고    scopus 로고
    • Conformation-dependent anti-amyloid oligomer antibodies
    • R. Kayed, and C.G. Glabe Conformation-dependent anti-amyloid oligomer antibodies Methods Enzymol 413 2006 326 344
    • (2006) Methods Enzymol , vol.413 , pp. 326-344
    • Kayed, R.1    Glabe, C.G.2
  • 14
    • 84886816046 scopus 로고    scopus 로고
    • Isolation, culture, and functional characterization of adult mouse cardiomyocytes
    • E.L. Graham, C. Balla, H. Franchino, Y. Melman, F. del Monte, and S. Das Isolation, culture, and functional characterization of adult mouse cardiomyocytes J Vis Exp 2013 e50289
    • (2013) J Vis Exp , pp. e50289
    • Graham, E.L.1    Balla, C.2    Franchino, H.3    Melman, Y.4    Del Monte, F.5    Das, S.6
  • 15
    • 0347357617 scopus 로고    scopus 로고
    • Protein folding and misfolding
    • C.M. Dobson Protein folding and misfolding Nature 426 2003 884 890
    • (2003) Nature , vol.426 , pp. 884-890
    • Dobson, C.M.1
  • 16
    • 0347987853 scopus 로고    scopus 로고
    • Folding proteins in fatal ways
    • D.J. Selkoe Folding proteins in fatal ways Nature 426 2003 900 904
    • (2003) Nature , vol.426 , pp. 900-904
    • Selkoe, D.J.1
  • 17
    • 84906065619 scopus 로고    scopus 로고
    • Protein post-translational modifications and misfolding: New concepts in heart failure
    • F. del Monte, and G. Agnetti Protein post-translational modifications and misfolding: new concepts in heart failure Proteomics Clin Appl 8 2014 534 542
    • (2014) Proteomics Clin Appl , vol.8 , pp. 534-542
    • Del Monte, F.1    Agnetti, G.2
  • 18
    • 0032565769 scopus 로고    scopus 로고
    • Cofilin phosphorylation by LIM-kinase 1 and its role in Rac-mediated actin reorganization
    • N. Yang, O. Higuchi, and K. Ohashi Cofilin phosphorylation by LIM-kinase 1 and its role in Rac-mediated actin reorganization Nature 393 1998 809 812
    • (1998) Nature , vol.393 , pp. 809-812
    • Yang, N.1    Higuchi, O.2    Ohashi, K.3
  • 19
    • 0037169335 scopus 로고    scopus 로고
    • Control of actin reorganization by Slingshot, a family of phosphatases that dephosphorylate ADF/cofilin
    • R. Niwa, K. Nagata-Ohashi, M. Takeichi, K. Mizuno, and T. Uemura Control of actin reorganization by Slingshot, a family of phosphatases that dephosphorylate ADF/cofilin Cell 108 2002 233 246
    • (2002) Cell , vol.108 , pp. 233-246
    • Niwa, R.1    Nagata-Ohashi, K.2    Takeichi, M.3    Mizuno, K.4    Uemura, T.5
  • 20
    • 12344250639 scopus 로고    scopus 로고
    • Chronophin, a novel HAD-type serine protein phosphatase, regulates cofilin-dependent actin dynamics
    • A. Gohla, J. Birkenfeld, and G.M. Bokoch Chronophin, a novel HAD-type serine protein phosphatase, regulates cofilin-dependent actin dynamics Nat Cell Biol 7 2005 21 29
    • (2005) Nat Cell Biol , vol.7 , pp. 21-29
    • Gohla, A.1    Birkenfeld, J.2    Bokoch, G.M.3
  • 22
    • 0027418205 scopus 로고
    • Measurement of co-localization of objects in dual-colour confocal images
    • Manders EEM, Verbeek FJ, Aten JA. Measurement of co-localization of objects in dual-colour confocal images. J Microsc 1993;169:375-82.
    • (1993) J Microsc , vol.169 , pp. 375-382
    • Manders, E.E.M.1    Verbeek, F.J.2    Aten, J.A.3
  • 23
    • 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
    • P.B. Agrawal, M. Joshi, T. Savic, Z. Chen, and A.H. Beggs 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 21 2012 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
  • 24
    • 84860738167 scopus 로고    scopus 로고
    • ADF/cofilin proteins translocate to mitochondria during apoptosis but are not generally required for cell death signaling
    • K. Rehklau, C.B. Gurniak, M. Conrad, E. Friauf, M. Ott, and M.B. Rust ADF/cofilin proteins translocate to mitochondria during apoptosis but are not generally required for cell death signaling Cell Death Differ 19 2012 958 967
    • (2012) Cell Death Differ , vol.19 , pp. 958-967
    • Rehklau, K.1    Gurniak, C.B.2    Conrad, M.3    Friauf, E.4    Ott, M.5    Rust, M.B.6
  • 25
    • 84868087341 scopus 로고    scopus 로고
    • Cofilin-1: A modulator of anxiety in mice
    • M. Goodson, M.B. Rust, and W. Witke Cofilin-1: a modulator of anxiety in mice PLoS Genet 8 2012 e1002970
    • (2012) PLoS Genet , vol.8 , pp. e1002970
    • Goodson, M.1    Rust, M.B.2    Witke, W.3
  • 26
    • 0032489871 scopus 로고    scopus 로고
    • Angiotensin II activates RhoA in cardiac myocytes: A critical role of RhoA in angiotensin II-induced premyofibril formation
    • H. Aoki, S. Izumo, and J. Sadoshima Angiotensin II activates RhoA in cardiac myocytes: a critical role of RhoA in angiotensin II-induced premyofibril formation Circ Res 82 1998 666 676
    • (1998) Circ Res , vol.82 , pp. 666-676
    • Aoki, H.1    Izumo, S.2    Sadoshima, J.3
  • 27
    • 70849098888 scopus 로고    scopus 로고
    • Actin, a central player in cell shape and movement
    • T.D. Pollard, and J.A. Cooper Actin, a central player in cell shape and movement Science 326 2009 1208 1212
    • (2009) Science , vol.326 , pp. 1208-1212
    • Pollard, T.D.1    Cooper, J.A.2
  • 28
    • 30544447666 scopus 로고    scopus 로고
    • Beta-secretase-cleaved amyloid precursor protein accumulates at actin inclusions induced in neurons by stress or amyloid beta: A feedforward mechanism for Alzheimer's disease
    • M.T. Maloney, L.S. Minamide, A.W. Kinley, J.A. Boyle, and J.R. Bamburg Beta-secretase-cleaved amyloid precursor protein accumulates at actin inclusions induced in neurons by stress or amyloid beta: a feedforward mechanism for Alzheimer's disease J Neurosci 25 2005 11313 11321
    • (2005) J Neurosci , vol.25 , pp. 11313-11321
    • Maloney, M.T.1    Minamide, L.S.2    Kinley, A.W.3    Boyle, J.A.4    Bamburg, J.R.5
  • 29
    • 33845977054 scopus 로고    scopus 로고
    • Nemaline myopathy with minicores caused by mutation of the CFL2 gene encoding the skeletal muscle actin-binding protein, cofilin-2
    • P.B. Agrawal, R.S. Greenleaf, and K.K. Tomczak Nemaline myopathy with minicores caused by mutation of the CFL2 gene encoding the skeletal muscle actin-binding protein, cofilin-2 Am J Hum Genet 80 2007 162 167
    • (2007) Am J Hum Genet , vol.80 , pp. 162-167
    • Agrawal, P.B.1    Greenleaf, R.S.2    Tomczak, K.K.3
  • 30
    • 84858246364 scopus 로고    scopus 로고
    • ADF/cofilin regulates actomyosin assembly through competitive inhibition of myosin II binding to F-actin
    • O. Wiggan, A.E. Shaw, J.G. DeLuca, and J.R. Bamburg ADF/cofilin regulates actomyosin assembly through competitive inhibition of myosin II binding to F-actin Dev Cell 22 2012 530 543
    • (2012) Dev Cell , vol.22 , pp. 530-543
    • Wiggan, O.1    Shaw, A.E.2    Deluca, J.G.3    Bamburg, J.R.4
  • 31
    • 84863113109 scopus 로고    scopus 로고
    • Actin stress fibers - Assembly, dynamics and biological roles
    • S. Tojkander, G. Gateva, and P. Lappalainen Actin stress fibers - assembly, dynamics and biological roles J Cell Sci 125 2012 1855 1864
    • (2012) J Cell Sci , vol.125 , pp. 1855-1864
    • Tojkander, S.1    Gateva, G.2    Lappalainen, P.3
  • 32
    • 33749512044 scopus 로고    scopus 로고
    • Alzheimer disease: Presenilin springs a leak
    • S. Gandy, M.K. Doeven, and B. Poolman Alzheimer disease: presenilin springs a leak Nat Med 12 2006 1121 1123
    • (2006) Nat Med , vol.12 , pp. 1121-1123
    • Gandy, S.1    Doeven, M.K.2    Poolman, B.3
  • 33
    • 77950859278 scopus 로고    scopus 로고
    • ADF/cofilin: A functional node in cell biology
    • B.W. Bernstein, and J.R. Bamburg ADF/cofilin: a functional node in cell biology Trends Cell Biol 20 2010 187 195
    • (2010) Trends Cell Biol , vol.20 , pp. 187-195
    • Bernstein, B.W.1    Bamburg, J.R.2
  • 34
    • 84895479294 scopus 로고    scopus 로고
    • Interplay of RhoA and mechanical forces in collective cell migration driven by leader cells
    • M. Reffay, M.C. Parrini, and O. Cochet-Escartin Interplay of RhoA and mechanical forces in collective cell migration driven by leader cells Nat Cell Biol 16 2014 217 223
    • (2014) Nat Cell Biol , vol.16 , pp. 217-223
    • Reffay, M.1    Parrini, M.C.2    Cochet-Escartin, O.3
  • 35
    • 0028799957 scopus 로고
    • Mutations in twinstar, a Drosophila gene encoding a cofilin/ADF homologue, result in defects in centrosome migration and cytokinesis
    • K.C. Gunsalus, S. Bonaccorsi, E. Williams, F. Verni, M. Gatti, and M.L. Goldberg Mutations in twinstar, a Drosophila gene encoding a cofilin/ADF homologue, result in defects in centrosome migration and cytokinesis J Cell Biol 131 1995 1243 1259
    • (1995) J Cell Biol , vol.131 , pp. 1243-1259
    • Gunsalus, K.C.1    Bonaccorsi, S.2    Williams, E.3    Verni, F.4    Gatti, M.5    Goldberg, M.L.6
  • 36
    • 0028955146 scopus 로고
    • Effects of cofilin on actin filamentous structures in cultured muscle cells. Intracellular regulation of cofilin action
    • R. Nagaoka, K. Kusano, H. Abe, and T. Obinata Effects of cofilin on actin filamentous structures in cultured muscle cells. Intracellular regulation of cofilin action J Cell Sci 108 Pt 2 1995 581 593
    • (1995) J Cell Sci , vol.108 , pp. 581-593
    • Nagaoka, R.1    Kusano, K.2    Abe, H.3    Obinata, T.4
  • 37
    • 84855932980 scopus 로고    scopus 로고
    • Cofilin activation mediates Bax translocation to mitochondria during excitotoxic neuronal death
    • I. Posadas, F.C. Perez-Martinez, J. Guerra, P. Sanchez-Verdu, and V. Cena Cofilin activation mediates Bax translocation to mitochondria during excitotoxic neuronal death J Neurochem 120 2012 515 527
    • (2012) J Neurochem , vol.120 , pp. 515-527
    • Posadas, I.1    Perez-Martinez, F.C.2    Guerra, J.3    Sanchez-Verdu, P.4    Cena, V.5


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