메뉴 건너뛰기




Volumn 24, Issue 1, 2013, Pages 31-41

Srv2/cyclase-associated protein forms hexameric shurikens that directly catalyze actin filament severing by cofilin

Author keywords

[No Author keywords available]

Indexed keywords

BINDING PROTEIN; COFILIN; CYCLASE ASSOCIATED PROTEIN; UNCLASSIFIED DRUG;

EID: 84871882289     PISSN: 10591524     EISSN: 19394586     Source Type: Journal    
DOI: 10.1091/mbc.E12-08-0589     Document Type: Article
Times cited : (86)

References (63)
  • 1
    • 33749046492 scopus 로고    scopus 로고
    • Mechanism of Actin Filament Turnover by Severing and Nucleation at Different Concentrations of ADF/Cofilin
    • DOI 10.1016/j.molcel.2006.08.006, PII S109727650600565X
    • Andrianantoandro E, Pollard TD (2006). Mechanism of actin filament turnover by severing and nucleation at different concentration of ADF/cofilin. Mol Cell 24, 13-23. (Pubitemid 44466682)
    • (2006) Molecular Cell , vol.24 , Issue.1 , pp. 13-23
    • Andrianantoandro, E.1    Pollard, T.D.2
  • 2
    • 0347664159 scopus 로고    scopus 로고
    • Coordinated Regulation of Actin Filament Turnover by a High-Molecular- Weight Srv2/CAP Complex, Cofilin, Profilin, and Aip1
    • DOI 10.1016/j.cub.2003.11.051
    • Balcer HI, Goodman AL, Rodal AA, Smith E, Kugler J, Heuser JE, Goode BL (2003). Coordinated regulation of actin filament turnover by a high-molecular weight Srv2/CAP complex, cofilin, profilin, and Aip1. Curr Biol 13, 2159-2169. (Pubitemid 38024940)
    • (2003) Current Biology , vol.13 , Issue.24 , pp. 2159-2169
    • Balcer, H.I.1    Goodman, A.L.2    Rodal, A.A.3    Smith, E.4    Kugler, J.5    Heuser, J.E.6    Goode, B.L.7
  • 3
    • 0034710563 scopus 로고    scopus 로고
    • A cyclase-associated protein regulates actin and cell polarity during Drosophila oogenesis and in yeast
    • Baum B, Li W, Perrimon N (2000). A cyclase-associated protein regulates actin and cell polarity during Drosophila oogenesis and in yeast. Curr Biol 10, 964-973.
    • (2000) Curr Biol , vol.10 , pp. 964-973
    • Baum, B.1    Li, W.2    Perrimon, N.3
  • 4
    • 77950859278 scopus 로고    scopus 로고
    • ADF/cofilin: A functional node in cell biology
    • Bernstein BW, Bamburg JR (2010). ADF/cofilin: a functional node in cell biology. Trends Cell Biol 20, 187-195.
    • (2010) Trends Cell Biol , vol.20 , pp. 187-195
    • Bernstein, B.W.1    Bamburg, J.R.2
  • 7
    • 30744462047 scopus 로고    scopus 로고
    • Cooperative effects of cofilin (ADF) on actin structure suggest allosteric mechanism of cofilin function
    • DOI 10.1016/j.jmb.2005.11.072, PII S0022283605015081
    • Bobkov AA, Muhlrad A, Pavlov DA, Kokabi K, Yilmaz A, Reisler E (2006). Cooperative effects of cofilin (ADF) on actin structure suggests allosteric mechanism of cofilin function. J Mol Biol 356, 325-334. (Pubitemid 43099974)
    • (2006) Journal of Molecular Biology , vol.356 , Issue.2 , pp. 325-334
    • Bobkov, A.A.1    Muhlrad, A.2    Pavlov, D.A.3    Kokabi, K.4    Yilmaz, A.5    Reisler, E.6
  • 8
    • 33750365532 scopus 로고    scopus 로고
    • Rapid actin monomer-insensitive depolymerization of Listeria actin comet tails by cofilin, coronin, and Aip1
    • DOI 10.1083/jcb.200603149
    • Brieher WM, Kueh HY, Ballif BA, Mitchison TJ (2006). Rapid actin monomer-insensitive depolymerization of Listeria actin comet tails by cofilin, coronin, and Aip1. J Cell Biol 175, 315-324. (Pubitemid 44631425)
    • (2006) Journal of Cell Biology , vol.175 , Issue.2 , pp. 315-324
    • Brieher, W.M.1    Hao, Y.K.2    Ballif, B.A.3    Mitchison, T.J.4
  • 9
    • 77952896939 scopus 로고    scopus 로고
    • Control of actin filament treadmilling in cell motility
    • Bugyi B, Carlier MF (2010). Control of actin filament treadmilling in cell motility. Annu Rev Biophys 39, 449-470.
    • (2010) Annu Rev Biophys , vol.39 , pp. 449-470
    • Bugyi, B.1    Carlier, M.F.2
  • 10
    • 52649120304 scopus 로고    scopus 로고
    • Coronin 1B antagonizes cortactin and remodels Arp2/3-containing actin branches in lamellipodia
    • Cai L, Makhov AM, Schafer DA, Bear JE (2008). Coronin 1B antagonizes cortactin and remodels Arp2/3-containing actin branches in lamellipodia. Cell 134, 828-842.
    • (2008) Cell , vol.134 , pp. 828-842
    • Cai, L.1    Makhov, A.M.2    Schafer, D.A.3    Bear, J.E.4
  • 12
    • 77951917756 scopus 로고    scopus 로고
    • A central role for the WH2 Domain of Srv2/CAP in recharging actin monomers to drive actin turnover in vitro and in vivo
    • Chaudhry F, Little K, Talarico L, Quintero-Monzon O, Goode BL (2010). A central role for the WH2 Domain of Srv2/CAP in recharging actin monomers to drive actin turnover in vitro and in vivo. Cytoskeleton 67, 120-133.
    • (2010) Cytoskeleton , vol.67 , pp. 120-133
    • Chaudhry, F.1    Little, K.2    Talarico, L.3    Quintero-Monzon, O.4    Goode, B.L.5
  • 13
    • 33845449481 scopus 로고    scopus 로고
    • SIGNATURE: A single-particle selection system for molecular electron microscopy
    • DOI 10.1016/j.jsb.2006.06.001, PII S1047847706001961, Software Tools for Macromolecular Microscopy
    • Chen JZ, Grigorieff N (2007). SIGNATURE: a single-particle selection system for molecular electron microscopy. J Struct Biol 157, 168-173. (Pubitemid 44895517)
    • (2007) Journal of Structural Biology , vol.157 , Issue.1 , pp. 168-173
    • Chen, J.Z.1    Grigorieff, N.2
  • 14
    • 77950022821 scopus 로고    scopus 로고
    • How cofilin severs an actin filament
    • De La Cruz EM (2009). How cofilin severs an actin filament. Biophys Rev 1, 51-59.
    • (2009) Biophys Rev , vol.1 , pp. 51-59
    • De La Cruz, E.M.1
  • 15
    • 77952196594 scopus 로고    scopus 로고
    • The kinetics of cooperative cofilin binding reveals two states of the cofilin-actin filament
    • De La Cruz EM, Sept DA (2010). The kinetics of cooperative cofilin binding reveals two states of the cofilin-actin filament. Biophys J 98, 1893-1901.
    • (2010) Biophys J , vol.98 , pp. 1893-1901
    • De La Cruz, E.M.1    Sept, D.A.2
  • 18
    • 56149087743 scopus 로고    scopus 로고
    • Intrinsic capability of budding yeast cofilin to promote turnover of tropomyosin-bound actin filaments
    • Fan X, Martin-Brown S, Florens L, Li R (2008). Intrinsic capability of budding yeast cofilin to promote turnover of tropomyosin-bound actin filaments. PLoS One 3, e3641.
    • (2008) PLoS One , vol.3
    • Fan, X.1    Martin-Brown, S.2    Florens, L.3    Li, R.4
  • 20
    • 65549103882 scopus 로고    scopus 로고
    • Coronin switches roles in actin assembly depending on the nucleotide state of actin
    • Gandhi M, Archard V, Blanchoin L, Goode BL (2009). Coronin switches roles in actin assembly depending on the nucleotide state of actin. Mol Cell 34, 364-374.
    • (2009) Mol Cell , vol.34 , pp. 364-374
    • Gandhi, M.1    Archard, V.2    Blanchoin, L.3    Goode, B.L.4
  • 21
    • 33845345287 scopus 로고    scopus 로고
    • Visualizing density maps with UCSF Chimera
    • DOI 10.1016/j.jsb.2006.06.010, PII S1047847706001948, Software Tools for Macromolecular Microscopy
    • Goddard TD, Huang CC, Ferrin TE (2007). Visualizing density maps with UCSF Chimera. J Struct Biol 157, 281-287. (Pubitemid 44880787)
    • (2007) Journal of Structural Biology , vol.157 , Issue.1 , pp. 281-287
    • Goddard, T.D.1    Huang, C.C.2    Ferrin, T.E.3
  • 22
    • 33845348200 scopus 로고    scopus 로고
    • FREALIGN: High-resolution refinement of single particle structures
    • Grigorieff N (2007). FREALIGN: high-resolution refinement of single particle structures. J Struct Biol 157, 117-125.
    • (2007) J Struct Biol , vol.157 , pp. 117-125
    • Grigorieff, N.1
  • 23
    • 0032992123 scopus 로고    scopus 로고
    • Cooperation of two actin-binding proteins, cofilin and Aip1, in Saccharomyces cerevisiae
    • Iida K, Yahara I (1999). Cooperation of two actin-binding proteins, cofilin and Aip1, in Saccharomyces cerevisiae. Genes Cells 4, 21-32. (Pubitemid 29151924)
    • (1999) Genes to Cells , vol.4 , Issue.1 , pp. 21-32
    • Iida, K.1    Yahara, I.2
  • 25
    • 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 (2008). Actin disassembly by cofilin, coronin, and Aip1 occurs in bursts and is inhibited by barbed-end cappers. J Cell Biol 182, 341-353.
    • (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
    • 18844389128 scopus 로고    scopus 로고
    • Real-time measurements of actin filament polymerization by total internal reflection fluorescence microscopy
    • DOI 10.1529/biophysj.104.047399
    • Kuhn JR, Pollard TD (2005). Real-time measurements of actin filament polymerization by total internal reflection fluorescence microscopy. Biophys J 88, 1387-1402. (Pubitemid 40975966)
    • (2005) Biophysical Journal , vol.88 , Issue.2 , pp. 1387-1402
    • Kuhn, J.R.1    Pollard, T.D.2
  • 27
    • 0030797467 scopus 로고    scopus 로고
    • Cofilin promotes rapid actin filament turnover in vivo
    • DOI 10.1038/40418
    • Lappalainen P, Drubin DG (1997). Cofilin promotes rapid actin filament turnover in vivo. Nature 388, 78-82. (Pubitemid 27283892)
    • (1997) Nature , vol.388 , Issue.6637 , pp. 78-82
    • Lappalainen, P.1    Drubin, D.G.2
  • 28
    • 0030880186 scopus 로고    scopus 로고
    • Essential functions and actin-binding surfaces of yeast cofilin revealed by systematic mutagenesis
    • DOI 10.1093/emboj/16.18.5520
    • Lappalainen P, Fedorov EV, Fedorov AA, Almo SC, Drubin DG (1997). Essential functions and actin-binding surfaces of yeast cofilin revealed by systematic mutagenesis. EMBO J 16, 5520-5530. (Pubitemid 27399844)
    • (1997) EMBO Journal , vol.16 , Issue.18 , pp. 5520-5530
    • Lappalainen, P.1    Fedorov, E.V.2    Fedorov, A.A.3    Almo, S.C.4    Drubin, D.G.5
  • 29
    • 42049092972 scopus 로고    scopus 로고
    • Regulation of actin assembly associated with protrusion and adhesion in cell migration
    • DOI 10.1152/physrev.00021.2007
    • Le Clainche C, Carlier MF (2008). Regulation of actin assembly associated with protrusion and adhesion in cell migration. Physiol Rev 88, 489-513. (Pubitemid 351520086)
    • (2008) Physiological Reviews , vol.88 , Issue.2 , pp. 489-513
    • Le, C.C.1    Carlier, M.-F.2
  • 30
    • 0024516197 scopus 로고
    • Disruption of the single tropomyosin gene in yeast results in the disappearance of actin cables from the cytoskeleton
    • Liu HP, Bretscher A (1989). Disruption of the single tropomyosin gene in yeast results in the disappearance of actin cables from the cytoskeleton. Cell 57, 233-242.
    • (1989) Cell , vol.57 , pp. 233-242
    • Liu, H.P.1    Bretscher, A.2
  • 31
    • 0026770695 scopus 로고
    • Characterization of TPM1 disrupted yeast cells indicates an involvement of tropomyosin in directed vesicular transport
    • Liu HP, Bretscher A (1992). Characterization of TPM1 disrupted yeast cells indicates an involvement of tropomyosin in directed vesicular transport. J Cell Biol 118, 285-299.
    • (1992) J Cell Biol , vol.118 , pp. 285-299
    • Liu, H.P.1    Bretscher, A.2
  • 32
    • 0026340941 scopus 로고
    • Characterization of actin filament severing by actophorin from Acanthamoeba castellanii
    • Maciver SK, Zot HG, Pollard TD (1991). Characterization of actin filament severing by actophorin from Acanthamoeba castellanii. J Cell Biol 115, 1611-1620. (Pubitemid 21910001)
    • (1991) Journal of Cell Biology , vol.115 , Issue.6 , pp. 1611-1620
    • Maciver, S.K.1    Zot, H.G.2    Pollard, T.D.3
  • 33
    • 6344225310 scopus 로고    scopus 로고
    • A high-affinity interaction with ADP-actin monomers underlies the mechanism and in vivo function of Srv2/cyclase-associated protein
    • DOI 10.1091/mbc.E04-06-0444
    • Mattila PK, Quintero-Monzon O, Kugler J, Moseley JB, Almo SC, Lappalainen P, Goode BL (2004). A high affinity interaction with ADP-actin monomers underlies the mechanism and in vivo function of Srv2/cyclase-associated protein (CAP). Mol Biol Cell 15, 5158-5171. (Pubitemid 39392227)
    • (2004) Molecular Biology of the Cell , vol.15 , Issue.11 , pp. 5158-5171
    • Mattila, P.K.1    Quintero-Monzon, O.2    Kugler, J.3    Moseley, J.B.4    Almo, S.C.5    Lappalainen, P.6    Goode, B.L.7
  • 34
    • 1542345783 scopus 로고    scopus 로고
    • NMR structural characterization of the N-terminal domain of the adenylyl cyclase-associated protein (CAP) from Dictyostelium discoideum
    • DOI 10.1023/B:JNMR.0000019513.86120.98
    • Mavoungou C, Israel L, Rehm T, Ksiazek D, Krajewski M, Popowicz G, Noegel A, Schleicher M, Holak T (2004). NMR structural characterization of the N-terminal domain of the adenylyl cyclase-associated protein (CAP) from Dictyostelium discoideum. J Biomol NMR 29, 73-84. (Pubitemid 38324875)
    • (2004) Journal of Biomolecular NMR , vol.29 , Issue.1 , pp. 73-84
    • Mavoungou, C.1    Israel, L.2    Rehm, T.3    Ksiazek, D.4    Krajewski, M.5    Popowicz, G.6    Noegel, A.A.7    Schleicher, M.8    Holak, T.A.9
  • 35
    • 80052476842 scopus 로고    scopus 로고
    • Cofilin-linked changes in actin filament flexibility promote severing
    • McCullough BR et al. (2011). Cofilin-linked changes in actin filament flexibility promote severing. Biophys J 101, 151-159.
    • (2011) Biophys J , vol.101 , pp. 151-159
    • McCullough, B.R.1
  • 36
    • 0030820734 scopus 로고    scopus 로고
    • Cofilin changes the twist of F-actin: Implications for actin filament dynamics and cellular function
    • DOI 10.1083/jcb.138.4.771
    • McGough A, Pope B, Chiu W, Weeds A (1997). Cofilin changes the twist of F-actin: implications for actin filament dynamics and cellular function. J Cell Biol 138, 771-781. (Pubitemid 27365041)
    • (1997) Journal of Cell Biology , vol.138 , Issue.4 , pp. 771-781
    • McGough, A.1    Pope, B.2    Chiu, W.3    Weeds, A.4
  • 37
    • 0242351058 scopus 로고    scopus 로고
    • Actin filament disassembling activity of Caenorhabditis elegans actin-interacting protein 1 (UNC-78) is dependent on filament binding by a specific ADF/cofilin isoform
    • DOI 10.1242/jcs.00717
    • Mohri K, Ono S (2003). Actin filament disassembling activity of Caenorhabditis elegans actin-interacting protein 1 (UNC-78) is dependent on filament binding by a specific ADF/cofilin isoform. J Cell Sci 116, 4107-4118. (Pubitemid 37337085)
    • (2003) Journal of Cell Science , vol.116 , Issue.20 , pp. 4107-4118
    • Mohri, K.1    Ono, S.2
  • 38
    • 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 (2002). Human CAP1 is a key factor in the recycling of cofilin and actin for rapid actin turnover. J Cell Sci 115, 1591-1601. (Pubitemid 34520589)
    • (2002) Journal of Cell Science , vol.115 , Issue.8 , pp. 1591-1601
    • Moriyama, K.1    Yahara, I.2
  • 40
    • 84867436458 scopus 로고    scopus 로고
    • Cyclase associated protein (CAP) acts directly on F-actin to accelerate cofilin-mediated actin severing across the range of physiological pH
    • Normoyle KPM, Brieher WM (2012). Cyclase associated protein (CAP) acts directly on F-actin to accelerate cofilin-mediated actin severing across the range of physiological pH. J Biol Chem 287, 35722-35732.
    • (2012) J Biol Chem , vol.287 , pp. 35722-35732
    • Normoyle, K.P.M.1    Brieher, W.M.2
  • 41
    • 0037044771 scopus 로고    scopus 로고
    • Xenopus actin-interacting protein 1 (XAip1) enhances cofilin fragmentation of filaments by capping filament ends
    • DOI 10.1074/jbc.M203111200
    • Okada K, Blanchoin L, Abe H, Chen H, Pollard TD, Bamburg JR (2002). Xenopus actin-interacting protein 1 (XAip1) enhances cofilin fragmentation of filaments by capping ends. J Biol Chem 277, 43011-43016. (Pubitemid 35285681)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.45 , pp. 43011-43016
    • Okada, K.1    Blanchoin, L.2    Abe, H.3    Chen, H.4    Pollard, T.D.5    Bamburg, J.R.6
  • 42
    • 0033050852 scopus 로고    scopus 로고
    • XAIP1: A Xenopus homologue of yeast actin interacting protein 1 (AIP1), which induces disassembly of actin filaments cooperatively with ADF/cofilin family proteins
    • Okada K, Obinata T, Abe H (1999). XAIP1: a Xenopus homologue of yeast actin interacting protein 1 (AIP1), which induces disassembly of actin filaments cooperatively with ADF cofilin family proteins. J Cell Sci 112, 1553-1565. (Pubitemid 29261317)
    • (1999) Journal of Cell Science , vol.112 , Issue.10 , pp. 1553-1565
    • Okada, K.1    Obinata, T.2    Abe, H.3
  • 43
    • 33745613278 scopus 로고    scopus 로고
    • Aip1 and cofilin promote rapid turnover of yeast actin patches and cables: A coordinated mechanism for severing and capping filaments
    • DOI 10.1091/mbc.E06-02-0135
    • Okada K, Ravi H, Smith EM, Goode BL (2006). Aip1 and cofilin promote rapid turnover of yeast actin patches and cables: a coordinated mechanism for severing and capping filaments. Mol Biol Cell 17, 2855-2868. (Pubitemid 43993492)
    • (2006) Molecular Biology of the Cell , vol.17 , Issue.7 , pp. 2855-2868
    • Okada, K.1    Ravi, H.2    Smith, E.M.3    Goode, B.L.4
  • 44
    • 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 D (2010). Loss of Aip1 reveals a role in maintaining the actin monomer pool and an in vivo oligomer assembly pathway. J Cell Biol 188, 769-777.
    • (2010) J Cell Biol , vol.188 , pp. 769-777
    • Okreglak, V.1    Drubin, D.2
  • 45
    • 1842790731 scopus 로고    scopus 로고
    • Microscopic Evidence That Actin-interacting Protein 1 Actively Disassembles Actin-depolymerizing Factor/Cofilin-bound Actin Filaments
    • DOI 10.1074/jbc.M313418200
    • Ono S, Mohri K, Ono K (2004). Microscopic evidence that actin-interacting protein 1 actively disassembles actin-depolymerizing factor/cofilin-bound actin filaments. J Biol Chem 279, 14207-14212. (Pubitemid 38468959)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.14 , pp. 14207-14212
    • Ono, S.1    Mohri, K.2    Ono, K.3
  • 47
    • 70849098888 scopus 로고    scopus 로고
    • Actin: A central player in cell shape and movement
    • Pollard TD, Cooper JA (2009). Actin: a central player in cell shape and movement. Science 326, 1208-1212.
    • (2009) Science , vol.326 , pp. 1208-1212
    • Pollard, T.D.1    Cooper, J.A.2
  • 48
    • 0032576569 scopus 로고    scopus 로고
    • Tropomyosin-containing actin cables direct the Myo2p-dependent polarized delivery of secretory vesicles in budding yeast
    • DOI 10.1083/jcb.143.7.1931
    • Pruyne DW, Schott DH, Bretscher A (1998). Tropomyosin-containing actin cables direct the Myo2p-dependent polarized delivery of secretory vesicles in budding yeast. J Cell Biol 143, 1931-1945. (Pubitemid 29022614)
    • (1998) Journal of Cell Biology , vol.143 , Issue.7 , pp. 1931-1945
    • Pruyne, D.W.1    Schott, D.H.2    Bretscher, A.3
  • 49
    • 67449107876 scopus 로고    scopus 로고
    • Reconstitution and dissection of the 600 kDa SRV2/CAP complex: Roles for oligomerization and cofilin-actin binding in driving actin turnover
    • Quintero-Monzon O, Jonasson EM, Bertling E, Talarico L, Chaudhry F, Sihvo M, Lappalainen P, Goode BL (2009). Reconstitution and dissection of the 600 kDa SRV2/CAP complex: roles for oligomerization and cofilin-actin binding in driving actin turnover. J Biol Chem 284, 10923-10934.
    • (2009) J Biol Chem , vol.284 , pp. 10923-10934
    • Quintero-Monzon, O.1    Jonasson, E.M.2    Bertling, E.3    Talarico, L.4    Chaudhry, F.5    Sihvo, M.6    Lappalainen, P.7    Goode, B.L.8
  • 51
    • 0141433278 scopus 로고    scopus 로고
    • Molecular requirements for actin-based lamella formation in Drosophila S2 cells
    • DOI 10.1083/jcb.200303023
    • Rogers SL, Wiedemann U, Stuurman N, Vale RD (2003). Molecular requirements for actin-based lamella formation in Drosophila S2 cells. J Cell Biol 162, 1079-1088. (Pubitemid 37174190)
    • (2003) Journal of Cell Biology , vol.162 , Issue.6 , pp. 1079-1088
    • Rogers, S.L.1    Wiedemann, U.2    Stuurman, N.3    Vale, R.D.4
  • 52
    • 0037033787 scopus 로고    scopus 로고
    • Secretory vesicle transport velocity in living cells depends on the myosin-V lever arm length
    • DOI 10.1083/jcb.200110086
    • Schott DH, Collins RN, Bretscher A (2002). Secretory vesicles transport velocity in living cells depends on the myosin-V lever arm length. J Cell Biol 156, 35-39. (Pubitemid 34846933)
    • (2002) Journal of Cell Biology , vol.156 , Issue.1 , pp. 35-39
    • Schott, D.H.1    Collins, R.N.2    Bretscher, A.3
  • 53
    • 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 JA, Watt S (1971). 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 246, 4866-4871.
    • (1971) J Biol Chem , vol.246 , pp. 4866-4871
    • Spudich, J.A.1    Watt, S.2
  • 55
    • 0025740949 scopus 로고
    • Actin microfilament dynamics in locomoting cells
    • Theriot JA, Mitchison TJ (1991). Actin microfilament dynamics in locomoting cells. Nature 352, 126-131. (Pubitemid 21896707)
    • (1991) Nature , vol.352 , Issue.6331 , pp. 126-131
    • Theriot, J.A.1    Mitchison, T.J.2
  • 56
    • 62849104599 scopus 로고    scopus 로고
    • An order of magnitude faster AIP1-associated actin disruption than nucleation by the Arp2/3 complex in lamellipodia
    • Tsuji T, Miyoshi T, Higashida C, Narumiya S, Watanabe N (2009). An order of magnitude faster AIP1-associated actin disruption than nucleation by the Arp2/3 complex in lamellipodia. PLoS One 4, e4921.
    • (2009) PLoS One , vol.4
    • Tsuji, T.1    Miyoshi, T.2    Higashida, C.3    Narumiya, S.4    Watanabe, N.5
  • 57
    • 0023102907 scopus 로고
    • Angular reconstitution: A posteriori assignment of projection directions for 3D reconstruction
    • Van Heel M (1987). Angular reconstitution: a posteriori assignment of projection directions for 3D reconstruction. Ultramicroscopy 21, 111-123.
    • (1987) Ultramicroscopy , vol.21 , pp. 111-123
    • Van Heel, M.1
  • 58
    • 0025989194 scopus 로고
    • Evidence for a functional link between profilin and CAP in the yeast S. cerevisiae
    • Vojtek A, Haarer B, Field J, Gerst J, Pollard TD, Brown S, Wigler M (1991). Evidence for a functional link between profilin and CAP in the yeast S. cerevisiae. Cell 66, 497-505. (Pubitemid 121001386)
    • (1991) Cell , vol.66 , Issue.3 , pp. 497-505
    • Vojtek, A.1    Haarer, B.2    Field, J.3    Gerst, J.4    Pollard, T.D.5    Brown, S.6    Wigler, M.7
  • 59
    • 0037039770 scopus 로고    scopus 로고
    • Single-molecule speckle analysis of actin filament turnover in lamellipodia
    • DOI 10.1126/science.1067470
    • Watanabe N, Mitchison TJ (2002). Single-molecule speckle analysis of actin filament turnover in lamellipodia. Science 295, 1083-1086. (Pubitemid 34132240)
    • (2002) Science , vol.295 , Issue.5557 , pp. 1083-1086
    • Watanabe, N.1    Mitchison, T.J.2
  • 60
    • 34447307946 scopus 로고    scopus 로고
    • Tropomyosin regulates elongation by formin at the fast-growing end of the actin filament
    • DOI 10.1021/bi700686p
    • Wawro B, Greenfield NJ, Wear MA, Cooper JA, Higgs HN, Hitchcock-DeGregori SE (2007). Tropomyosin regulates elongation by formin at the fast-growing end of the actin filament. Biochemistry 46, 8146-8155. (Pubitemid 47051650)
    • (2007) Biochemistry , vol.46 , Issue.27 , pp. 8146-8155
    • Wawro, B.1    Greenfield, N.J.2    Wear, M.A.3    Cooper, J.A.4    Higgs, H.N.5    Hitchcock-DeGregori, S.E.6
  • 61
    • 63449127854 scopus 로고    scopus 로고
    • Adenylate cyclase-associated protein 1 overexpressed in pancreatic cancers is involved in cancer cell motility
    • Yamazaki K et al. (2009). Adenylate cyclase-associated protein 1 overexpressed in pancreatic cancers is involved in cancer cell motility. Lab Invest 89, 425-432.
    • (2009) Lab Invest , vol.89 , pp. 425-432
    • Yamazaki, K.1
  • 62
    • 11344253088 scopus 로고    scopus 로고
    • Structural evidence for variable oligomerization of the N-terminal domain of cyclase-associated protein (CAP)
    • DOI 10.1002/prot.20314
    • Yusof A, Hu N-J, Wlodawer A, Hofmann A (2005). Structural evidence for variable oligomerization of the N-terminal domain of cyclase-associated protein (CAP). Proteins 58, 255-262. (Pubitemid 40076040)
    • (2005) Proteins: Structure, Function and Genetics , vol.58 , Issue.2 , pp. 255-262
    • Yusof, A.M.1    Hu, N.-J.2    Wlodawer, A.3    Hofmann, A.4
  • 63
    • 33748463918 scopus 로고    scopus 로고
    • Mechanism of Oligomerisation of Cyclase-associated Protein from Dictyostelium discoideum in Solution
    • DOI 10.1016/j.jmb.2006.08.008, PII S002228360600996X
    • Yusof A, Jaenicke E, Pedersen JS, Noegel AA, Schleicher M, Hofmann A (2006). Mechanism of oligomerisation of cyclase-associated protein from Dictyostelium discoideum in solution. J Mol Biol 362, 1072-1081. (Pubitemid 44353527)
    • (2006) Journal of Molecular Biology , vol.362 , Issue.5 , pp. 1072-1081
    • Yusof, A.M.1    Jaenicke, E.2    Pedersen, J.S.3    Noegel, A.A.4    Schleicher, M.5    Hofmann, A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.