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Volumn 22, Issue 20, 2011, Pages 3826-3839

The functionally distinct fission yeast formins have specific actin-assembly properties

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; CELL CYCLE PROTEIN; CELL CYCLE PROTEIN 12; CELL PROTEIN; FUNGAL PROTEIN; PROFILIN; PROTEIN FOR3; PROTEIN FUS1; UNCLASSIFIED DRUG;

EID: 80054714234     PISSN: 10591524     EISSN: 19394586     Source Type: Journal    
DOI: 10.1091/mbc.E11-06-0492     Document Type: Article
Times cited : (39)

References (69)
  • 1
    • 0034720293 scopus 로고    scopus 로고
    • Direct observation of dendritic actin filament networks nucleated by Arp2/3 complex and WASP/Scar proteins
    • DOI 10.1038/35010008
    • Blanchoin L, Amann KJ, Higgs HN, Marchand JB, Kaiser DA, Pollard TD (2000). Direct observation of dendritic actin filament networks nucleated by Arp2/3 complex and WASP/Scar proteins. Nature 404, 1007-1011. (Pubitemid 30243596)
    • (2000) Nature , vol.404 , Issue.6781 , pp. 1007-1011
    • Blancholn, L.1    Amann, K.J.2    Higgs, H.N.3    Marchand, J.-B.4    Kaiser, D.A.5    Pollard, T.D.6
  • 2
    • 0028053435 scopus 로고
    • diaphanous is required for cytokinesis in Drosophila and shares domains of similarity with the products of the limb deformity gene
    • Castrillon DH, Wasserman SA (1994). diaphanous is required for cytokinesis in Drosophila and shares domains of similarity with the products of the limb deformity gene. Development 120, 3367-3377. (Pubitemid 24366983)
    • (1994) Development , vol.120 , Issue.12 , pp. 3367-3377
    • Castrillon, D.H.1    Wasserman, S.A.2
  • 3
    • 0030958087 scopus 로고    scopus 로고
    • cdc12p, a protein required for cytokinesis in fission yeast, is a component of the cell division ring and interacts with profilin
    • DOI 10.1083/jcb.137.1.169
    • Chang F, Drubin D, Nurse P (1997). cdc12p, a protein required for cytokinesis in fission yeast, is a component of the cell division ring and interacts with profilin. J Cell Biol 137, 169-182. (Pubitemid 27167304)
    • (1997) Journal of Cell Biology , vol.137 , Issue.1 , pp. 169-182
    • Chang, F.1    Drubin, D.2    Nurse, P.3
  • 4
    • 73849086549 scopus 로고    scopus 로고
    • Roles of formin nodes and myosin motor activity in Mid1p-dependent contractile-ring assembly during fission yeast cytokinesis
    • Coffman VC, Nile AH, Lee IJ, Liu H, Wu JQ (2009). Roles of formin nodes and myosin motor activity in Mid1p-dependent contractile-ring assembly during fission yeast cytokinesis. Mol Biol Cell 20, 5195-5210.
    • (2009) Mol Biol Cell , vol.20 , pp. 5195-5210
    • Coffman, V.C.1    Nile, A.H.2    Lee, I.J.3    Liu, H.4    Wu, J.Q.5
  • 5
    • 0020533805 scopus 로고
    • Pyrene actin: documentation of the validity of a sensitive assay for actin polymerization
    • Cooper JA, Walker SB, Pollard TD (1983). Pyrene actin: documentation of the validity of a sensitive assay for actin polymerization. J Muscle Res Cell Motil 4, 253-262. (Pubitemid 13069975)
    • (1983) Journal of Muscle Research and Cell Motility , vol.4 , Issue.2 , pp. 253-262
    • Cooper, J.A.1    Walker, S.B.2    Pollard, T.D.3
  • 6
    • 0035975991 scopus 로고    scopus 로고
    • Roles of the fission yeast formin for3p in cell polarity, actin cable formation and symmetric cell division
    • DOI 10.1016/S0960-9822(01)00525-5
    • Feierbach B, Chang F (2001). Roles of the fission yeast formin for3p in cell polarity, actin cable formation and symmetric cell division. Curr Biol 11, 1656-1665. (Pubitemid 33037776)
    • (2001) Current Biology , vol.11 , Issue.21 , pp. 1656-1665
    • Feierbach, B.1    Chang, F.2
  • 7
    • 34248154652 scopus 로고    scopus 로고
    • Mechanism and function of formins in the control of actin assembly
    • Goode BL, Eck MJ (2007). Mechanism and function of formins in the control of actin assembly. Annu Rev Biochem 76, 593-627.
    • (2007) Annu Rev Biochem , vol.76 , pp. 593-627
    • Goode, B.L.1    Eck, M.J.2
  • 9
    • 0025977037 scopus 로고
    • Eukaryotic proteins expressed in Escherichia coli: An improved thrombin cleavage and purification procedure of fusion proteins with glutathione S-transferase
    • Guan KL, Dixon JE (1991). Eukaryotic proteins expressed in Escherichia coli: an improved thrombin cleavage and purification procedure of fusion proteins with glutathione S-transferase. Anal Biochem 192, 262-267.
    • (1991) Anal Biochem , vol.192 , pp. 262-267
    • Guan, K.L.1    Dixon, J.E.2
  • 10
    • 33646867122 scopus 로고    scopus 로고
    • Mechanistic differences in actin bundling activity of two mammalian formins, FRL1 and mDia2
    • DOI 10.1074/jbc.M510923200
    • Harris ES, Rouiller I, Hanein D, Higgs HN (2006). Mechanistic differences in actin bundling activity of two mammalian formins, FRL1 and mDia2. J Biol Chem 281, 14383-14392. (Pubitemid 43848368)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.20 , pp. 14383-14392
    • Harris, E.S.1    Rouiller, I.2    Hanein, D.3    Higgs, H.N.4
  • 11
    • 18844438774 scopus 로고    scopus 로고
    • Formin proteins: A domain-based approach
    • Higgs HN (2005). Formin proteins: a domain-based approach. Trends Biochem Sci 30, 342-353.
    • (2005) Trends Biochem Sci , vol.30 , pp. 342-353
    • Higgs, H.N.1
  • 12
    • 11144281883 scopus 로고    scopus 로고
    • Phylogenetic analysis of the formin homology 2 domain
    • DOI 10.1091/mbc.E04-07-0565
    • Higgs HN, Peterson KJ (2005). Phylogenetic analysis of the formin homology 2 domain. Mol Biol Cell 16, 1-13. (Pubitemid 40024285)
    • (2005) Molecular Biology of the Cell , vol.16 , Issue.1 , pp. 1-13
    • Higgs, H.N.1    Peterson, K.J.2
  • 13
    • 0016294918 scopus 로고
    • The measurement of actin concentration in solution: A comparison of methods
    • Houk TW Jr, Ue K (1974). The measurement of actin concentration in solution: a comparison of methods. Anal Biochem 62, 66-74.
    • (1974) Anal Biochem , vol.62 , pp. 66-74
    • Houk Jr., T.W.1    Ue, K.2
  • 14
    • 26944432407 scopus 로고    scopus 로고
    • Directionality of F-actin cables changes during the fission yeast cell cycle
    • DOI 10.1038/ncb1295, PII N1295
    • Kamasaki T, Arai R, Osumi M, Mabuchi I (2005). Directionality of F-actin cables changes during the fission yeast cell cycle. Nat Cell Biol 7, 916-917. (Pubitemid 41486293)
    • (2005) Nature Cell Biology , vol.7 , Issue.9 , pp. 916-917
    • Kamasaki, T.1    Arai, R.2    Osumi, M.3    Mabuchi, I.4
  • 15
    • 34548299090 scopus 로고    scopus 로고
    • Three-dimensional arrangement of F-actin in the contractile ring of fission yeast
    • DOI 10.1083/jcb.200612018
    • Kamasaki T, Osumi M, Mabuchi I (2007). Three-dimensional arrangement of F-actin in the contractile ring of fission yeast. J Cell Biol 178, 765-771. (Pubitemid 47347362)
    • (2007) Journal of Cell Biology , vol.178 , Issue.5 , pp. 765-771
    • Kamasaki, T.1    Osumi, M.2    Mabuchi, I.3
  • 16
    • 30844449003 scopus 로고    scopus 로고
    • Molecular details of formin-mediated actin assembly
    • Kovar DR (2006). Molecular details of formin-mediated actin assembly. Curr Opin Cell Biol 18, 11-17.
    • (2006) Curr Opin Cell Biol , vol.18 , pp. 11-17
    • Kovar, D.R.1
  • 17
    • 80054682072 scopus 로고    scopus 로고
    • Carlier MF (2010). Formin-mediated actin assembly
    • ed. MF Carlier, New York: Springer
    • Kovar DR, Bestul AJ, Li Y, Scott BJ (2010). Carlier MF (2010). Formin-mediated actin assembly. In: Actin-based Motility, ed. MF Carlier, New York: Springer, 279-316.
    • (2010) Actin-based Motility , pp. 279-316
    • Kovar, D.R.1    Bestul, A.J.2    Li, Y.3    Scott, B.J.4
  • 18
    • 31044433924 scopus 로고    scopus 로고
    • Control of the assembly of ATP- and ADP-actin by formins and profilin
    • DOI 10.1016/j.cell.2005.11.038, PII S009286740501398X
    • Kovar DR, Harris ES, Mahaffy R, Higgs HN, Pollard TD (2006). Control of the assembly of ATP- and ADP-actin by formins and profilin. Cell 124, 423-435. (Pubitemid 43121988)
    • (2006) Cell , vol.124 , Issue.2 , pp. 423-435
    • Kovar, D.R.1    Harris, E.S.2    Mahaffy, R.3    Higgs, H.N.4    Pollard, T.D.5
  • 19
    • 0037780973 scopus 로고    scopus 로고
    • The fission yeast cytokinesis formin Cdc12p is a barbed end actin filament capping protein gated by profilin
    • DOI 10.1083/jcb.200211078
    • Kovar DR, Kuhn JR, Tichy AL, Pollard TD (2003). The fission yeast cytokinesis formin Cdc12p is a barbed end actin filament capping protein gated by profilin. J Cell Biol 161, 875-887. (Pubitemid 36718421)
    • (2003) Journal of Cell Biology , vol.161 , Issue.5 , pp. 875-887
    • Kovar, D.R.1    Kuhn, J.R.2    Tichy, A.L.3    Pollard, T.D.4
  • 21
    • 79952104296 scopus 로고    scopus 로고
    • Three's company: The fission yeast actin cytoskeleton
    • Kovar DR, Sirotkin V, Lord M (2011). Three's company: the fission yeast actin cytoskeleton. Trends Cell Biol 21, 177-187.
    • (2011) Trends Cell Biol , vol.21 , pp. 177-187
    • Kovar, D.R.1    Sirotkin, V.2    Lord, M.3
  • 22
    • 18244377374 scopus 로고    scopus 로고
    • Profilin-mediated competition between capping protein and formin Cdc12p during cytokinesis in fission yeast
    • DOI 10.1091/mbc.E04-09-0781
    • Kovar DR, Wu JQ, Pollard TD (2005). Profilin-mediated competition between capping protein and formin Cdc12p during cytokinesis in fission yeast. Mol Biol Cell 16, 2313-2324. (Pubitemid 40632214)
    • (2005) Molecular Biology of the Cell , vol.16 , Issue.5 , pp. 2313-2324
    • Kovar, D.R.1    Wu, J.-Q.2    Pollard, T.D.3
  • 23
    • 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
  • 24
    • 36348984486 scopus 로고    scopus 로고
    • High-resolution Structural Analysis of Mammalian Profilin 2a Complex Formation with Two Physiological Ligands: The Formin Homology 1 Domain of mDia1 and the Proline-rich Domain of VASP
    • DOI 10.1016/j.jmb.2007.10.050, PII S0022283607013861
    • Kursula P, Kursula I, Massimi M, Song YH, Downer J, Stanley WA, Witke W, Wilmanns M (2008). High-resolution structural analysis of mammalian profilin 2a complex formation with two physiological ligands: the formin homology 1 domain of mDia1 and the proline-rich domain of VASP. J Mol Biol 375, 270-290. (Pubitemid 350160700)
    • (2008) Journal of Molecular Biology , vol.375 , Issue.1 , pp. 270-290
    • Kursula, P.1    Kursula, I.2    Massimi, M.3    Song, Y.-H.4    Downer, J.5    Stanley, W.A.6    Witke, W.7    Wilmanns, M.8
  • 25
    • 79955509029 scopus 로고    scopus 로고
    • Assembly and architecture of precursor nodes during fission yeast cytokinesis
    • Laporte D, Coffman VC, Lee IJ, Wu JQ (2011). Assembly and architecture of precursor nodes during fission yeast cytokinesis. J Cell Biol 192, 1005-1021.
    • (2011) J Cell Biol , vol.192 , pp. 1005-1021
    • Laporte, D.1    Coffman, V.C.2    Lee, I.J.3    Wu, J.Q.4
  • 26
    • 0035163855 scopus 로고    scopus 로고
    • Profilin binding to poly-L-proline and actin monomers along with ability to catalyze actin nucleotide exchange is required for viability of fission yeast
    • Lu J, Pollard TD (2001). Profilin binding to poly-l-proline and actin monomers along with ability to catalyze actin nucleotide exchange is required for viability of fission yeast. Mol Biol Cell 12, 1161-1175. (Pubitemid 33052006)
    • (2001) Molecular Biology of the Cell , vol.12 , Issue.4 , pp. 1161-1175
    • Lu, J.1    Pollard, T.D.2
  • 27
    • 33745003433 scopus 로고    scopus 로고
    • Dynamics of the Formin For3p in Actin Cable Assembly
    • DOI 10.1016/j.cub.2006.04.040, PII S0960982206015375
    • Martin SG, Chang F (2006). Dynamics of the formin for3p in actin cable assembly. Curr Biol 16, 1161-1170. (Pubitemid 43867291)
    • (2006) Current Biology , vol.16 , Issue.12 , pp. 1161-1170
    • Martin, S.G.1    Chang, F.2
  • 30
    • 23044510466 scopus 로고    scopus 로고
    • Differential activities and regulation of Saccharomyces cerevisiae formin proteins Bni1 and Bnr1 by Bud6
    • DOI 10.1074/jbc.M503094200
    • Moseley JB, Goode BL (2005). Differential activities and regulation of Saccharomyces cerevisiae formin proteins Bni1 and Bnr1 by Bud6. J Biol Chem 280, 28023-28033. (Pubitemid 41076920)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.30 , pp. 28023-28033
    • Moseley, J.B.1    Goode, B.L.2
  • 31
    • 0742305302 scopus 로고    scopus 로고
    • A Conserved Mechanism for Bni1- and mDia1-induced Actin Assembly and Dual Regulation of Bni1 by Bud6 and Profilin
    • DOI 10.1091/mbc.E03-08-0621
    • Moseley JB, Sagot I, Manning AL, Xu Y, Eck MJ, Pellman D, Goode BL (2004). A conserved mechanism for Bni1- and mDia1-induced actin assembly and dual regulation of Bni1 by Bud6 and profilin. Mol Biol Cell 15, 896-907. (Pubitemid 38146502)
    • (2004) Molecular Biology of the Cell , vol.15 , Issue.2 , pp. 896-907
    • Moseley, J.B.1    Sagot, I.2    Manning, A.L.3    Xu, Y.4    Eck, M.J.5    Pellman, D.6    Goode, B.L.7
  • 32
    • 12244291296 scopus 로고    scopus 로고
    • The small GTPase Rho3 and the diaphanous/formin For3 function in polarized cell growth in fission yeast
    • DOI 10.1242/jcs.00150
    • Nakano K, Imai J, Arai R, Toh EA, Matsui Y, Mabuchi I (2002). The small GTPase Rho3 and the diaphanous/formin For3 function in polarized cell growth in fission yeast. J Cell Sci 115, 4629-4639. (Pubitemid 36004422)
    • (2002) Journal of Cell Science , vol.115 , Issue.23 , pp. 4629-4639
    • Nakano, K.1    Imai, J.2    Arai, R.3    Toh-e, A.4    Matsui, Y.5    Mabuchi, I.6
  • 33
    • 0035192626 scopus 로고    scopus 로고
    • Interactions among a fimbrin, a capping protein, and an actin-depolymerizing factor in organization of the fission yeast actin cytoskeleton
    • Nakano K, Satoh K, Morimatsu A, Ohnuma M, Mabuchi I (2001). Interactions among a fimbrin, a capping protein, and an actin-depolymerizing factor in organization of the fission yeast actin cytoskeleton. Mol Biol Cell 12, 3515-3526. (Pubitemid 33108483)
    • (2001) Molecular Biology of the Cell , vol.12 , Issue.11 , pp. 3515-3526
    • Nakano, K.1    Satoh, K.2    Morimatsu, A.3    Ohnuma, M.4    Mabuchi, I.5
  • 34
    • 58649122903 scopus 로고    scopus 로고
    • Formin differentially utilizes pro- filin isoforms to rapidly assemble actin filaments
    • Neidt EM, Scott BJ, Kovar DR (2009). Formin differentially utilizes pro- filin isoforms to rapidly assemble actin filaments. J Biol Chem 284, 673-684.
    • (2009) J Biol Chem , vol.284 , pp. 673-684
    • Neidt, E.M.1    Scott, B.J.2    Kovar, D.R.3
  • 35
    • 53049093335 scopus 로고    scopus 로고
    • The cytokinesis formins from the nematode worm and fission yeast differentially mediate actin filament assembly
    • Neidt EM, Skau CT, Kovar DR (2008). The cytokinesis formins from the nematode worm and fission yeast differentially mediate actin filament assembly. J Biol Chem 283, 23872-23883.
    • (2008) J Biol Chem , vol.283 , pp. 23872-23883
    • Neidt, E.M.1    Skau, C.T.2    Kovar, D.R.3
  • 36
    • 20844439387 scopus 로고    scopus 로고
    • Structural basis of Rho GTPase-mediated activation of the formin mDia1
    • DOI 10.1016/j.molcel.2005.04.002, PII S1097276505012268
    • Otomo T, Otomo C, Tomchick DR, Machius M, Rosen MK (2005a). Structural basis of Rho GTPase-mediated activation of the formin mDia1. Mol Cell 18, 273-281. (Pubitemid 41350533)
    • (2005) Molecular Cell , vol.18 , Issue.3 , pp. 273-281
    • Otomo, T.1    Otomo, C.2    Tomchick, D.R.3    Machius, M.4    Rosen, M.K.5
  • 37
    • 13444280218 scopus 로고    scopus 로고
    • Structural basis of actin filament nucleation and processive capping by a formin homology 2 domain
    • DOI 10.1038/nature03251
    • Otomo T, Tomchick DR, Otomo C, Panchal SC, Machius M, Rosen MK (2005b). Structural basis of actin filament nucleation and processive capping by a formin homology 2 domain. Nature 433, 488-494. (Pubitemid 40204299)
    • (2005) Nature , vol.433 , Issue.7025 , pp. 488-494
    • Otomo, T.1    Tomchick, D.R.2    Otomo, C.3    Panchal, S.C.4    Machius, M.5    Rosen, M.K.6
  • 38
    • 0035886026 scopus 로고    scopus 로고
    • 2, ADP-actin monomers, and capping protein regulate the activity and localization of yeast twinfilin
    • DOI 10.1083/jcb.200106157
    • Palmgren S, Ojala PJ, Wear MA, Cooper JA, Lappalainen P (2001). Interactions with PIP2, ADP-actin monomers, and capping protein regulate the activity and localization of yeast twinfilin. J Cell Biol 155, 251-260. (Pubitemid 34289300)
    • (2001) Journal of Cell Biology , vol.155 , Issue.2 , pp. 251-260
    • Palmgren, S.1    Ojala, P.J.2    Wear, M.A.3    Cooper, J.A.4    Lappalainen, P.5
  • 39
    • 40149105917 scopus 로고    scopus 로고
    • The role of the FH1 domain and profilin in formin-mediated actin-filament elongation and nucleation
    • Paul AS, Pollard TD (2008). The role of the FH1 domain and profilin in formin-mediated actin-filament elongation and nucleation. Curr Biol 18, 9-19.
    • (2008) Curr Biol , vol.18 , pp. 9-19
    • Paul, A.S.1    Pollard, T.D.2
  • 40
    • 66449124043 scopus 로고    scopus 로고
    • Energetic requirements for processive elongation of actin filaments by FH1FH2 formins
    • Paul AS, Pollard TD (2009a). Energetic requirements for processive elongation of actin filaments by FH1FH2 formins. J Biol Chem 284, 12533-12540.
    • (2009) J Biol Chem , vol.284 , pp. 12533-12540
    • Paul, A.S.1    Pollard, T.D.2
  • 41
    • 67749135871 scopus 로고    scopus 로고
    • Review of the mechanism of processive actin filament elongation by formins
    • Paul AS, Pollard TD (2009b). Review of the mechanism of processive actin filament elongation by formins. Cell Motil Cytoskeleton 66, 606-617.
    • (2009) Cell Motil Cytoskeleton , vol.66 , pp. 606-617
    • Paul, A.S.1    Pollard, T.D.2
  • 42
    • 0027991942 scopus 로고
    • Interaction of profilin with G-actin and poly(L-proline)
    • DOI 10.1021/bi00194a011
    • Perelroizen I, Marchand JB, Blanchoin L, Didry D, Carlier MF (1994). Interaction of profilin with G-actin and poly(L-proline). Biochemistry 33, 8472-8478. (Pubitemid 24242684)
    • (1994) Biochemistry , vol.33 , Issue.28 , pp. 8472-8478
    • Perelroizen, I.1    Marchand, J.-B.2    Blanchoin, L.3    Didry, D.4    Carlier, M.-F.5
  • 43
    • 0031966898 scopus 로고    scopus 로고
    • F-actin distribution and function during sexual differentiation in Schizosaccharomyces pombe
    • Petersen J, Nielsen O, Egel R, Hagan IM (1998a). F-actin distribution and function during sexual differentiation in Schizosaccharomyces pombe. J Cell Sci 111, 867-876. (Pubitemid 28196070)
    • (1998) Journal of Cell Science , vol.111 , Issue.7 , pp. 867-876
    • Petersen, J.1    Nielsen, O.2    Egel, R.3    Hagan, L.M.4
  • 44
    • 0032101410 scopus 로고    scopus 로고
    • FH3, a domain found in formins, targets the fission yeast formin Fus1 to the projection tip during conjugation
    • DOI 10.1083/jcb.141.5.1217
    • Petersen J, Nielsen O, Egel R, Hagan IM (1998b). FH3, a domain found in formins, targets the fission yeast formin Fus1 to the projection tip during conjugation. J Cell Biol 141, 1217-1228. (Pubitemid 28265615)
    • (1998) Journal of Cell Biology , vol.141 , Issue.5 , pp. 1217-1228
    • Petersen, J.1    Nielsen, O.2    Egel, R.3    Hagan, I.M.4
  • 45
    • 0029019950 scopus 로고
    • Characterization of fus1 of Schizosaccharomyces pombe: A developmentally controlled function needed for conjugation
    • Petersen J, Weilguny D, Egel R, Nielsen O (1995). Characterization of fus1 of Schizosaccharomyces pombe: a developmentally controlled function needed for conjugation. Mol Cell Biol 15, 3697-3707.
    • (1995) Mol Cell Biol , vol.15 , pp. 3697-3707
    • Petersen, J.1    Weilguny, D.2    Egel, R.3    Nielsen, O.4
  • 46
    • 0030475459 scopus 로고    scopus 로고
    • Structural requirements and thermodynamics of the interaction of proline peptides with profilin
    • DOI 10.1021/bi961498d
    • Petrella EC, Machesky LM, Kaiser DA, Pollard TD (1996). Structural requirements and thermodynamics of the interaction of proline peptides with profilin. Biochemistry 35, 16535-16543. (Pubitemid 27020495)
    • (1996) Biochemistry , vol.35 , Issue.51 , pp. 16535-16543
    • Petrella, E.C.1    Machesky, L.M.2    Kaiser, D.A.3    Pollard, T.D.4
  • 47
    • 0037458002 scopus 로고    scopus 로고
    • Mechanism of formin-induced nucleation of actin filaments
    • DOI 10.1021/bi026520j
    • Pring M, Evangelista M, Boone C, Yang C, Zigmond SH (2003). Mechanism of formin-induced nucleation of actin filaments. Biochemistry 42, 486-496. (Pubitemid 36105767)
    • (2003) Biochemistry , vol.42 , Issue.2 , pp. 486-496
    • Pring, M.1    Evangelista, M.2    Boone, C.3    Yang, C.4    Zigmond, S.H.5
  • 48
    • 0037178706 scopus 로고    scopus 로고
    • Role of formins in actin assembly: Nucleation and barbed-end association
    • DOI 10.1126/science.1072309
    • Pruyne D, Evangelista M, Yang C, Bi E, Zigmond S, Bretscher A, Boone C (2002). Role of formins in actin assembly: nucleation and barbed-end association. Science 297, 612-615. (Pubitemid 34815347)
    • (2002) Science , vol.297 , Issue.5581 , pp. 612-615
    • Pruyne, D.1    Evangelista, M.2    Yang, C.3    Bi, E.4    Zigmond, S.5    Bretscher, A.6    Boone, C.7
  • 49
    • 20444381052 scopus 로고    scopus 로고
    • A comparative sequence analysis reveals a common GBD/FH3- FH1-FH2-DAD architecture in formins from Dictyostelium, fungi and metazoa
    • Rivero F, Muramoto T, Meyer AK, Urushihara H, Uyeda TQ, Kitayama C (2005). A comparative sequence analysis reveals a common GBD/FH3- FH1-FH2-DAD architecture in formins from Dictyostelium, fungi and metazoa. BMC Genomics 6, 28.
    • (2005) BMC Genomics , vol.6 , pp. 28
    • Rivero, F.1    Muramoto, T.2    Meyer, A.K.3    Urushihara, H.4    Uyeda, T.Q.5    Kitayama, C.6
  • 50
    • 7044224754 scopus 로고    scopus 로고
    • Formin is a processive motor that requires profilin to accelerate actin assembly and associated ATP hydrolysis
    • DOI 10.1016/j.cell.2004.09.039, PII S0092867404009365
    • Romero S, Le Clainche C, Didry D, Egile C, Pantaloni D, Carlier MF (2004). Formin is a processive motor that requires profilin to accelerate actin assembly and associated ATP hydrolysis. Cell 119, 419-429. (Pubitemid 39423843)
    • (2004) Cell , vol.119 , Issue.3 , pp. 419-429
    • Romero, S.1    Le, C.C.2    Didry, D.3    Egile, C.4    Pantaloni, D.5    Carlier, M.-F.6
  • 52
    • 77649273530 scopus 로고    scopus 로고
    • Fifteen formins for an actin filament: A molecular view on the regulation of human formins
    • Schonichen A, Geyer M (2010). Fifteen formins for an actin filament: a molecular view on the regulation of human formins. Biochim Biophys Acta 1803, 152-163.
    • (2010) Biochim Biophys Acta , vol.1803 , pp. 152-163
    • Schonichen, A.1    Geyer, M.2
  • 53
    • 79960666093 scopus 로고    scopus 로고
    • Actin filament bundling by fimbrin is important for endocytosis, cytokinesis, and polarization in fission yeast
    • Skau CT, Courson DS, Bestul AJ, Winkelman JD, Rock RS, Sirotkin V, Kovar DR (2011). Actin filament bundling by fimbrin is important for endocytosis, cytokinesis, and polarization in fission yeast. J Biol Chem 286, 26964-77.
    • (2011) J Biol Chem , vol.286 , pp. 26964-26977
    • Skau, C.T.1    Courson, D.S.2    Bestul, A.J.3    Winkelman, J.D.4    Rock, R.S.5    Sirotkin, V.6    Kovar, D.R.7
  • 54
    • 77957850795 scopus 로고    scopus 로고
    • Fimbrin and tropomyosin competition regulates endocytosis and cytokinesis kinetics in fission yeast
    • Skau CT, Kovar DR (2010). Fimbrin and tropomyosin competition regulates endocytosis and cytokinesis kinetics in fission yeast. Curr Biol 20, 1415-1422.
    • (2010) Curr Biol , vol.20 , pp. 1415-1422
    • Skau, C.T.1    Kovar, D.R.2
  • 55
    • 65249102795 scopus 로고    scopus 로고
    • Role of tropomyosin in formin-mediated contractile ring assembly in fission yeast
    • Skau CT, Neidt EM, Kovar DR (2009). Role of tropomyosin in formin-mediated contractile ring assembly in fission yeast. Mol Biol Cell 20, 2160-2173.
    • (2009) Mol Biol Cell , vol.20 , pp. 2160-2173
    • Skau, C.T.1    Neidt, E.M.2    Kovar, D.R.3
  • 56
    • 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
  • 58
    • 34547593312 scopus 로고    scopus 로고
    • Properties of actin from the fission yeast Schizosaccharomyces pombe and interaction with fission yeast profilin
    • DOI 10.1074/jbc.M611371200
    • Takaine M, Mabuchi I (2007). Properties of actin from fission yeast Schizosaccharomyces pombe and interaction with fission yeast profilin. J Biol Chem 282, 21683-21694. (Pubitemid 47195769)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.30 , pp. 21683-21694
    • Takaine, M.1    Mabuchi, I.2
  • 59
    • 70350304803 scopus 로고    scopus 로고
    • Fission yeast IQGAP arranges actin filaments into the cytokinetic contractile ring
    • Takaine M, Numata O, Nakano K (2009). Fission yeast IQGAP arranges actin filaments into the cytokinetic contractile ring. EMBO J 28, 3117-3131.
    • (2009) EMBO J , vol.28 , pp. 3117-3131
    • Takaine, M.1    Numata, O.2    Nakano, K.3
  • 60
    • 79953148555 scopus 로고    scopus 로고
    • Purification of actin from fission yeast Schizosaccharomyces pombe and characterization of functional differences from muscle actin
    • Ti SC, Pollard TD (2011). Purification of actin from fission yeast Schizosaccharomyces pombe and characterization of functional differences from muscle actin. J Biol Chem 286, 5784-5792.
    • (2011) J Biol Chem , vol.286 , pp. 5784-5792
    • Ti, S.C.1    Pollard, T.D.2
  • 61
    • 31044443763 scopus 로고    scopus 로고
    • Model of formin-associated actin filament elongation
    • DOI 10.1016/j.molcel.2006.01.016, PII S1097276506000384
    • Vavylonis D, Kovar DR, O'Shaughnessy B, Pollard TD (2006). Model of formin-associated actin filament elongation. Mol Cell 21, 455-466. (Pubitemid 43228002)
    • (2006) Molecular Cell , vol.21 , Issue.4 , pp. 455-466
    • Vavylonis, D.1    Kovar, D.R.2    O'Shaughnessy, B.3    Pollard, T.D.4
  • 62
    • 37849017207 scopus 로고    scopus 로고
    • Assembly mechanism of the contractile ring for cytokinesis by fission yeast
    • Vavylonis D, Wu JQ, Hao S, O'Shaughnessy B, Pollard TD (2008). Assembly mechanism of the contractile ring for cytokinesis by fission yeast. Science 319, 97-100.
    • (2008) Science , vol.319 , pp. 97-100
    • Vavylonis, D.1    Wu, J.Q.2    Hao, S.3    O'Shaughnessy, B.4    Pollard, T.D.5
  • 64
    • 58149345827 scopus 로고    scopus 로고
    • Model of For3p-mediated actin cable assembly in fission yeast
    • Wang H, Vavylonis D (2008). Model of For3p-mediated actin cable assembly in fission yeast. PLoS One 3, e4078.
    • (2008) PLoS One , vol.3
    • Wang, H.1    Vavylonis, D.2
  • 65
    • 0035158574 scopus 로고    scopus 로고
    • Roles of a fimbrin and an á-actinin-like protein in fission yeast cell polarization and cytokinesis
    • Wu JQ, Bahler J, Pringle JR (2001). Roles of a fimbrin and an á-actinin-like protein in fission yeast cell polarization and cytokinesis. Mol Biol Cell 12, 1061-1077. (Pubitemid 33051999)
    • (2001) Molecular Biology of the Cell , vol.12 , Issue.4 , pp. 1061-1077
    • Wu, J.-Q.1    Bahler, J.2    Pringle, J.R.3
  • 67
    • 1542269073 scopus 로고    scopus 로고
    • Crystal structures of a formin homology-2 domain reveal a tethered dimer architecture
    • DOI 10.1016/S0092-8674(04)00210-7, PII S0092867404002107
    • Xu Y, Moseley JB, Sagot I, Poy F, Pellman D, Goode BL, Eck MJ (2004). Crystal structures of a formin homology-2 domain reveal a tethered dimer architecture. Cell 116, 711-723. (Pubitemid 38326729)
    • (2004) Cell , vol.116 , Issue.5 , pp. 711-723
    • Xu, Y.1    Moseley, J.B.2    Sagot, I.3    Poy, F.4    Pellman, D.5    Goode, B.L.6    Eck, M.J.7
  • 68
    • 77949488512 scopus 로고    scopus 로고
    • Regulation of cytokinesis by the formin cdc12p
    • Yonetani A, Chang F (2010). Regulation of cytokinesis by the formin cdc12p. Curr Biol 20, 561-566.
    • (2010) Curr Biol , vol.20 , pp. 561-566
    • Yonetani, A.1    Chang, F.2


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