메뉴 건너뛰기




Volumn 2, Issue 1, 2010, Pages

Roles of ADF/cofilin in actin polymerization and beyond

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; CHAPERONE; COFILIN; CYTOCHROME C; F ACTIN; MITOCHONDRIAL ENZYME; PHOSPHOLIPASE D1;

EID: 78649373184     PISSN: 17404118     EISSN: 1757594X     Source Type: Journal    
DOI: 10.3410/B2-62     Document Type: Review
Times cited : (148)

References (38)
  • 2
    • 0036304481 scopus 로고    scopus 로고
    • Determining the differences in actin binding by human ADF and cofilin
    • DOI 10.1006/jmbi.2001.5280
    • Yeoh S, Pope B, Mannherz HG, Weeds AG: Determining the differences in actin binding by human ADF and cofilin. J Mol Biol 2002, 315:911-25. (Pubitemid 34729336)
    • (2002) Journal of Molecular Biology , vol.315 , Issue.4 , pp. 911-925
    • Yeoh, S.1    Pope, B.2    Mannherz, H.G.3    Weeds, A.4
  • 3
    • 2642580847 scopus 로고    scopus 로고
    • In vitro activity differences between proteins of the ADF/cofilin family define two distinct subgroups
    • Chen H, Bernstein BW, Sneider JM, Boyle JA, Minamide LS, Bamburg JR: In vitro activity differences between proteins of the ADF/cofilin family define two distinct subgroups. Biochemistry 2004, 43:7127-42.
    • (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
  • 4
    • 12844269159 scopus 로고    scopus 로고
    • Actin-depolymerizing factor and cofilin-1 play overlapping roles in promoting rapid F-actin depolymerization in mammalian nonmuscle cells
    • Hotulainen P, Paunola E, Vartianen MK, Lappalainen P: Actin-depolymerizing factor and cofilin-1 play overlapping roles in promoting rapid F-actin depolymerization in mammalian nonmuscle cells. Mol Biol Cell 2005, 16:649-64.
    • (2005) Mol Biol Cell , vol.16 , pp. 649-664
    • Hotulainen, P.1    Paunola, E.2    Vartianen, M.K.3    Lappalainen, P.4
  • 6
    • 11844276055 scopus 로고    scopus 로고
    • The actin depolymerizing factor n-cofilin is essential for neural tube morphogenesis and neural crest cell migration
    • DOI 10.1016/j.ydbio.2004.11.010, PII S0012160604008024
    • Gurniak CB, Perlas E, Witke W: The actin depolymerizing factor n-cofilin is essential for neural tube morphogenesis and neural crest cell migration. Dev Biol 2005, 278:231-41. (Pubitemid 40092863)
    • (2005) Developmental Biology , vol.278 , Issue.1 , pp. 231-241
    • Gurniak, C.B.1    Perlas, E.2    Witke, W.3
  • 7
    • 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 LA, Bogess D, Hawes N, Hobson CD, Sundberg JP, Naggert JK, Smith RS, Nishina PM: Aberrant actin cytoskeleton leads to accelerated proliferation of corneal epithelial cells in mice deficient for destrin (actin depolymerizing factor). Hum Mol Genet 2003, 12:1029-37.
    • (2003) Hum Mol Genet , vol.12 , pp. 1029-1037
    • Ikeda, S.1    Cunningham, L.A.2    Bogess, 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
  • 8
    • 33749046492 scopus 로고    scopus 로고
    • Mechanism of actin filament turnover by severing and nucleation at different concentrations of ADF/cofilin
    • Andrianantoandro E, Pollard TD: 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
  • 10
    • 77950859278 scopus 로고    scopus 로고
    • ADF/cofilin: A functional node in cell biology
    • Bernstein BW, Bamburg JR: ADF/cofilin: a functional node in cell biology. Trends Cell Biol 2010, 20:187-95.
    • (2010) Trends Cell Biol , vol.20 , pp. 187-195
    • Bernstein, B.W.1    Bamburg, J.R.2
  • 11
    • 77949679483 scopus 로고    scopus 로고
    • Loss of Aip1 reveals a role in maintaining the actin monomer pool and an in vivo oligomer assembly pathway
    • Okreglak V, Drubin DG: Loss of Aip1 reveals a role in maintaining the actin monomer pool and an in vivo oligomer assembly pathway. J Cell Biol 2010, 188:769-77.
    • (2010) J Cell Biol , vol.188 , pp. 769-777
    • Okreglak, V.1    Drubin, D.G.2
  • 12
    • 60849116466 scopus 로고    scopus 로고
    • Tropomyosin and ADF/cofilin as collaborators and competitors
    • Kuhn TB, Bamburg JR: Tropomyosin and ADF/cofilin as collaborators and competitors. Adv Exp Med Biol 2008, 644:232-49.
    • (2008) Adv Exp Med Biol , vol.644 , pp. 232-249
    • Kuhn, T.B.1    Bamburg, J.R.2
  • 13
    • 0033060250 scopus 로고    scopus 로고
    • Mechanism of interaction of Acanthamoeba actophorin (ADF/cofilin) with actin filaments
    • Blanchoin L, Pollard TD: Mechanism of interaction of Acanthamoeba actophorin (ADF/cofilin) with actin filaments. J Biol Chem 1999, 274:15538-46. (Pubitemid 129518907)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.22 , pp. 15538-15546
    • Blanchoin, L.1    Pollard, T.D.2
  • 14
    • 71749095987 scopus 로고    scopus 로고
    • The cofilin activity cycle in lamellipodia and invadopodia
    • Oser M, Condeelis J: The cofilin activity cycle in lamellipodia and invadopodia. J Cell Biochem 2009, 108:1256-62.
    • (2009) J Cell Biochem , vol.108 , pp. 1256-1262
    • Oser, M.1    Condeelis, J.2
  • 17
    • 64049091643 scopus 로고    scopus 로고
    • Cofilin dissociates Arp2/3 complex and branches from actin filaments
    • Chan C, Beltzner CC, Pollard TD: Cofilin dissociates Arp2/3 complex and branches from actin filaments. Curr Biol 2009, 19:537-45.
    • (2009) Curr Biol , vol.19 , pp. 537-545
    • Chan, C.1    Beltzner, C.C.2    Pollard, T.D.3
  • 18
    • 14644399182 scopus 로고    scopus 로고
    • The motility of glioblastoma tumour cells is modulated by intracellular cofilin expression in a concentration-dependent manner
    • Yap CT, Simpson TI, Pratt T, Price DJ, Maciver SK: The motility of glioblastoma tumour cells is modulated by intracellular cofilin expression in a concentration-dependent manner. Cell Motil Cytoskeleton 2005, 60:153-65.
    • (2005) Cell Motil Cytoskeleton , vol.60 , pp. 153-165
    • Yap, C.T.1    Simpson, T.I.2    Pratt, T.3    Price, D.J.4    Maciver, S.K.5
  • 19
    • 33644530393 scopus 로고    scopus 로고
    • Par-3 mediates the inhibition of LIM kinase 2 to regulate cofilin phosphorylation and tight junction assembly
    • Chen X, Macara IG: Par-3 mediates the inhibition of LIM kinase 2 to regulate cofilin phosphorylation and tight junction assembly. J Cell Biol 2006, 172:671-8.
    • (2006) J Cell Biol , vol.172 , pp. 671-678
    • Chen, X.1    Macara, I.G.2
  • 20
    • 33750489040 scopus 로고    scopus 로고
    • Tyrosine phosphorylated Par3 regulates epithelial tight junction assembly promoted by EGFR signaling
    • DOI 10.1038/sj.emboj.7601384, PII 7601384
    • Wang Y, Du D, Fang L, Yang G, Zhang C, Zheng R, Ullrich A, Lottspeich F, Chen Z: Tyrosine phopshorylated Par3 regulates epithelial tight junction assembly promoted by EGFR signaling. EMBO J 2006, 25:5058-70. (Pubitemid 44658524)
    • (2006) EMBO Journal , vol.25 , Issue.21 , pp. 5058-5070
    • Wang, Y.1    Du, D.2    Fang, L.3    Yang, G.4    Zhang, C.5    Zeng, R.6    Ullrich, A.7    Lottspeich, F.8    Chen, Z.9
  • 21
    • 38349046975 scopus 로고    scopus 로고
    • ADF/cofilin family proteins control formation of oriented actin-filament bundles in the cell body to trigger fibroblast polarization
    • Mseka T, Bamburg JR, Cramer LP: ADF/cofilin family proteins control formation of oriented actin-filament bundles in the cell body to trigger fibroblast polarization. J Cell Sci 2007, 120:4332-44.
    • (2007) J Cell Sci , vol.120 , pp. 4332-4344
    • Mseka, T.1    Bamburg, J.R.2    Cramer, L.P.3
  • 22
    • 33847420825 scopus 로고    scopus 로고
    • Coronin 1B coordinates Arp2/3 complex and cofilin activities at the leading edge
    • Cai L, Marshall TW, Uetrecht AC, Schafer DA, Bear JE: Coronin 1B coordinates Arp2/3 complex and cofilin activities at the leading edge. Cell 2007, 128:915-29.
    • (2007) Cell , vol.128 , pp. 915-929
    • Cai, L.1    Marshall, T.W.2    Uetrecht, A.C.3    Schafer, D.A.4    Bear, J.E.5
  • 23
    • 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 BL: Coronin switches roles in actin disassembly depending on the nucleotide state of actin. Mol Cell 2009, 34:364-74.
    • (2009) Mol Cell , vol.34 , pp. 364-374
    • Gandhi, M.1    Achard, V.2    Blanchoin, L.3    Goode, B.L.4
  • 24
    • 48249121534 scopus 로고    scopus 로고
    • Actin disassembly by cofilin, coronin, and Aip1 occurs in bursts and is inhibited by barbed-end cappers
    • Kueh HY, Charras GT, Mitchison TJ, Brieher WM: Actin disassembly by cofilin, coronin, and Aip1 occurs in bursts and is inhibited by barbed-end cappers. J Cell Biol 2008, 182:341-53.
    • (2008) J Cell Biol , vol.182 , pp. 341-353
    • Kueh, H.Y.1    Charras, G.T.2    Mitchison, T.J.3    Brieher, W.M.4
  • 26
    • 0033588258 scopus 로고    scopus 로고
    • ADF/cofilin weakens lateral contacts in the actin filament
    • DOI 10.1006/jmbi.1999.2968
    • McGough A, Chiu W: ADF/cofilin weakens lateral contacts in the actin filament. J Mol Biol 1999, 291:513-19. (Pubitemid 29392629)
    • (1999) Journal of Molecular Biology , vol.291 , Issue.3 , pp. 513-519
    • McGough, A.1    Chiu, W.2
  • 27
    • 65349161753 scopus 로고    scopus 로고
    • Nuclear actin and actin-binding proteins in the regulation of transcription and gene expression
    • Zheng B, Han M, Bernier M, Wen JK: Nuclear actin and actin-binding proteins in the regulation of transcription and gene expression. FEBS J 2009, 276:2669-85.
    • (2009) FEBS J , vol.276 , pp. 2669-2685
    • Zheng, B.1    Han, M.2    Bernier, M.3    Wen, J.K.4
  • 31
    • 77956646000 scopus 로고    scopus 로고
    • ADF/cofilin binds phosphoinositides in a multivalent manner to act as a PIP(2)-density sensor
    • Zhao H, Hakala M, Lappalainen P: ADF/cofilin binds phosphoinositides in a multivalent manner to act as a PIP(2)-density sensor. Biophys J 2010, 98:2327-36.
    • (2010) Biophys J , vol.98 , pp. 2327-2336
    • Zhao, H.1    Hakala, M.2    Lappalainen, P.3
  • 33
    • 74449092215 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of cofilin at Y68 by v-Src leads to its degradation through ubiquitin-proteasome pathway
    • Yoo Y, Ho HJ, Wang C, Guan JL: Tyrosine phosphorylation of cofilin at Y68 by v-Src leads to its degradation through ubiquitin-proteasome pathway. Oncogene 2009, 29:263-72.
    • (2009) Oncogene , vol.29 , pp. 263-272
    • Yoo, Y.1    Ho, H.J.2    Wang, C.3    Guan, J.L.4
  • 34
    • 51349166966 scopus 로고    scopus 로고
    • Oxidation of cofilin mediates T cell hyporesponsiveness under oxidative stress conditions
    • Klemke M, Wabnitz GH, Funke F, Funk B, Kirchgessner H, Samstag Y: Oxidation of cofilin mediates T cell hyporesponsiveness under oxidative stress conditions. Immunity 2008, 29:404-13.
    • (2008) Immunity , vol.29 , pp. 404-413
    • Klemke, M.1    Wabnitz, G.H.2    Funke, F.3    Funk, B.4    Kirchgessner, H.5    Samstag, Y.6
  • 35
    • 67649822159 scopus 로고    scopus 로고
    • Regulation of acetylcholine receptor clustering by ADF/cofilin-directed vesicular trafficking
    • Lee CW, Han J, Bamburg JR, Han L, Lynn R, Zheng JQ: Regulation of acetylcholine receptor clustering by ADF/cofilin-directed vesicular trafficking. Nat Neurosci 2009, 12:848-56.
    • (2009) Nat Neurosci , vol.12 , pp. 848-856
    • Lee, C.W.1    Han, J.2    Bamburg, J.R.3    Han, L.4    Lynn, R.5    Zheng, J.Q.6
  • 36
    • 58149379613 scopus 로고    scopus 로고
    • SynGAP regulates steady-state and activity-dependent phosphorylation of cofilin
    • Carlisle HJ, Manzerra P, Marcora E, Kennedy MB: SynGAP regulates steady-state and activity-dependent phosphorylation of cofilin. J Neurosci 2008, 28:13673-83.
    • (2008) J Neurosci , vol.28 , pp. 13673-13683
    • Carlisle, H.J.1    Manzerra, P.2    Marcora, E.3    Kennedy, M.B.4
  • 37
    • 77954484950 scopus 로고    scopus 로고
    • Regulation of AMPA receptor channels and synaptic plasticity by cofilin phosphatase slingshot in cortical neurons
    • Yuen EY, Liu W, Kafri T, Van Praag H, Yan Z: Regulation of AMPA receptor channels and synaptic plasticity by cofilin phosphatase slingshot in cortical neurons. J Physiol 2010, 588:2661-71.
    • (2010) J Physiol , vol.588 , pp. 2661-2671
    • Yuen, E.Y.1    Liu, W.2    Kafri, T.3    Van Praag, H.4    Yan, Z.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.