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Volumn 4, Issue , 2012, Pages 31-47

Actin filament nucleation and elongation

Author keywords

Actin polymerization; Arp2 3 complex; Cobl; Elongation; Eva VASP; Formin; Lmod; Nucleation; Spire; VopL VopF

Indexed keywords


EID: 84882798898     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1016/B978-0-12-374920-8.00404-5     Document Type: Chapter
Times cited : (4)

References (153)
  • 1
    • 0037459075 scopus 로고    scopus 로고
    • Cellular motility driven by assembly and disassembly of actin filaments
    • Pollard T.D., Borisy G.G. Cellular motility driven by assembly and disassembly of actin filaments. Cell 2003, 112:453-465.
    • (2003) Cell , vol.112 , pp. 453-465
    • Pollard, T.D.1    Borisy, G.G.2
  • 2
    • 42049092972 scopus 로고    scopus 로고
    • Regulation of actin assembly associated with protrusion and adhesion in cell migration
    • Le Clainche C., Carlier M.F. Regulation of actin assembly associated with protrusion and adhesion in cell migration. Physiol Rev. 2008, 88:489-513.
    • (2008) Physiol Rev. , vol.88 , pp. 489-513
    • Le Clainche, C.1    Carlier, M.F.2
  • 3
    • 60749098725 scopus 로고    scopus 로고
    • Actin and endocytosis: mechanisms and phylogeny
    • Galletta B.J., Cooper J.A. Actin and endocytosis: mechanisms and phylogeny. Curr. Opin. Cell Biol. 2009, 21:20-27.
    • (2009) Curr. Opin. Cell Biol. , vol.21 , pp. 20-27
    • Galletta, B.J.1    Cooper, J.A.2
  • 4
    • 34848927902 scopus 로고    scopus 로고
    • The many faces of actin: matching assembly factors with cellular structures
    • Chhabra E.S., Higgs H.N. The many faces of actin: matching assembly factors with cellular structures. Nat. Cell Biol. 2007, 9:1110-1121.
    • (2007) Nat. Cell Biol. , vol.9 , pp. 1110-1121
    • Chhabra, E.S.1    Higgs, H.N.2
  • 5
    • 35348992048 scopus 로고    scopus 로고
    • Manipulation of host-cell pathways by bacterial pathogens
    • Bhavsar A.P., Guttman J.A., Finlay B.B. Manipulation of host-cell pathways by bacterial pathogens. Nature 2007, 449:827-834.
    • (2007) Nature , vol.449 , pp. 827-834
    • Bhavsar, A.P.1    Guttman, J.A.2    Finlay, B.B.3
  • 6
    • 53449094756 scopus 로고    scopus 로고
    • Listeria monocytogenes, a unique model in infection biology: an overview
    • Cossart P., Toledo-Arana A. Listeria monocytogenes, a unique model in infection biology: an overview. Microbes Infect. 2008, 10:1041-1050.
    • (2008) Microbes Infect. , vol.10 , pp. 1041-1050
    • Cossart, P.1    Toledo-Arana, A.2
  • 8
    • 0034896467 scopus 로고    scopus 로고
    • Thermodynamics and kinetics of actin filament nucleation
    • Sept D., McCammon J.A. Thermodynamics and kinetics of actin filament nucleation. Biophys. J. 2001, 81:667-674.
    • (2001) Biophys. J. , vol.81 , pp. 667-674
    • Sept, D.1    McCammon, J.A.2
  • 9
    • 60749122102 scopus 로고    scopus 로고
    • Actin nucleation and elongation factors: mechanisms and interplay
    • Chesarone M.A., Goode B.L. Actin nucleation and elongation factors: mechanisms and interplay. Curr. Opin. Cell Biol. 2009, 21:28-37.
    • (2009) Curr. Opin. Cell Biol. , vol.21 , pp. 28-37
    • Chesarone, M.A.1    Goode, B.L.2
  • 10
    • 66349133039 scopus 로고    scopus 로고
    • New players in actin polymerization: WH2-domain-containing actin nucleators
    • Qualmann B., Kessels M.M. New players in actin polymerization: WH2-domain-containing actin nucleators. Trends Cell Biol. 2009, 19:276-285.
    • (2009) Trends Cell Biol. , vol.19 , pp. 276-285
    • Qualmann, B.1    Kessels, M.M.2
  • 11
    • 52949096103 scopus 로고    scopus 로고
    • Spire and Cordon-bleu: multifunctional regulators of actin dynamics
    • Renault L., Bugyi B., Carlier M.F. Spire and Cordon-bleu: multifunctional regulators of actin dynamics. Trends Cell Biol. 2008, 18:494-504.
    • (2008) Trends Cell Biol. , vol.18 , pp. 494-504
    • Renault, L.1    Bugyi, B.2    Carlier, M.F.3
  • 12
    • 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
  • 13
    • 34248154652 scopus 로고    scopus 로고
    • Mechanism and function of formins in the control of actin assembly
    • Goode B.L., Eck M.J. Mechanism and function of formins in the control of actin assembly. Annu. Rev. Biochem. 2007, 76:593-627.
    • (2007) Annu. Rev. Biochem. , vol.76 , pp. 593-627
    • Goode, B.L.1    Eck, M.J.2
  • 14
    • 33749037156 scopus 로고    scopus 로고
    • The ARP2/3 complex: an actin nucleator comes of age
    • Goley E.D., Welch M.D. The ARP2/3 complex: an actin nucleator comes of age. Nat. Rev. Mol. Cell Biol. 2006, 7:713-726.
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , pp. 713-726
    • Goley, E.D.1    Welch, M.D.2
  • 15
    • 33646864565 scopus 로고    scopus 로고
    • Staying in shape with formins
    • Faix J., Grosse R. Staying in shape with formins. Dev. Cell 2006, 10:693-706.
    • (2006) Dev. Cell , vol.10 , pp. 693-706
    • Faix, J.1    Grosse, R.2
  • 16
    • 18844438774 scopus 로고    scopus 로고
    • Formin proteins: a domain-based approach
    • Higgs H.N. Formin proteins: a domain-based approach. Trends Biochem. Sci. 2005, 30:342-353.
    • (2005) Trends Biochem. Sci. , vol.30 , pp. 342-353
    • Higgs, H.N.1
  • 17
    • 67749135871 scopus 로고    scopus 로고
    • Review of the mechanism of processive actin filament elongation by formins
    • Paul A.S., Pollard T.D. Review of the mechanism of processive actin filament elongation by formins. Cell Motil. Cytoskeleton 2009, 66:606-617.
    • (2009) Cell Motil. Cytoskeleton , vol.66 , pp. 606-617
    • Paul, A.S.1    Pollard, T.D.2
  • 18
    • 77951272888 scopus 로고    scopus 로고
    • Structural insights into de novo actin polymerization
    • Dominguez R. Structural insights into de novo actin polymerization. Curr. Opin. Struct. Biol. 2010, 20:217-225.
    • (2010) Curr. Opin. Struct. Biol. , vol.20 , pp. 217-225
    • Dominguez, R.1
  • 19
    • 70450245305 scopus 로고    scopus 로고
    • Actin filament nucleation and elongation factors: structure-function relationships
    • Dominguez R. Actin filament nucleation and elongation factors: structure-function relationships. Crit. Rev. Biochem. Mol. Biol. 2009, 44:351-366.
    • (2009) Crit. Rev. Biochem. Mol. Biol. , vol.44 , pp. 351-366
    • Dominguez, R.1
  • 20
    • 77949834455 scopus 로고    scopus 로고
    • A nucleator arms race: cellular control of actin assembly
    • Campellone K.G., Welch M.D. A nucleator arms race: cellular control of actin assembly. Nat. Rev. Mol. Cell Biol. 2010, 11:237-251.
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 237-251
    • Campellone, K.G.1    Welch, M.D.2
  • 21
    • 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
  • 22
    • 77957996302 scopus 로고    scopus 로고
    • Direct visualisation of secondary structures of F-actin by electron cryomicroscopy
    • Fujii, T.; Iwane, A.H.; Yanagida, T.; Namba, K. Direct visualisation 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
  • 23
    • 0022881322 scopus 로고
    • Rate constants for the reactions of ATP- and ADP-actin with the ends of actin filaments
    • Pollard T.D. Rate constants for the reactions of ATP- and ADP-actin with the ends of actin filaments. J. Cell Biol. 1986, 103:2747-2754.
    • (1986) J. Cell Biol. , vol.103 , pp. 2747-2754
    • Pollard, T.D.1
  • 24
    • 0019358370 scopus 로고
    • The first step in the polymerisation of actin
    • Rouayrenc J.F., Travers F. The first step in the polymerisation of actin. Eur. J. Biochem. 1981, 116:73-77.
    • (1981) Eur. J. Biochem. , vol.116 , pp. 73-77
    • Rouayrenc, J.F.1    Travers, F.2
  • 25
    • 0026520541 scopus 로고
    • Chemical evidence for the existence of activated G-actin
    • Shu W.P., Wang D., Stracher A. Chemical evidence for the existence of activated G-actin. Biochem. J. 1992, 283(Pt 2):567-573.
    • (1992) Biochem. J. , vol.283 , Issue.PT 2 , pp. 567-573
    • Shu, W.P.1    Wang, D.2    Stracher, A.3
  • 26
    • 0020146091 scopus 로고
    • Mechanism of K+-induced actin assembly
    • Pardee J.D., Spudich J.A. Mechanism of K+-induced actin assembly. J. Cell Biol. 1982, 93:648-654.
    • (1982) J. Cell Biol. , vol.93 , pp. 648-654
    • Pardee, J.D.1    Spudich, J.A.2
  • 28
    • 0037080339 scopus 로고    scopus 로고
    • Hydrolysis of ATP by polymerized actin depends on the bound divalent cation but not profilin
    • Blanchoin L., Pollard T.D. Hydrolysis of ATP by polymerized actin depends on the bound divalent cation but not profilin. Biochemistry 2002, 41:597-602.
    • (2002) Biochemistry , vol.41 , pp. 597-602
    • Blanchoin, L.1    Pollard, T.D.2
  • 29
    • 0022876860 scopus 로고
    • Direct evidence for ADP-Pi-F-actin as the major intermediate in ATP-actin polymerization: rate of dissociation of Pi from actin filaments
    • Carlier M.F., Pantaloni D. Direct evidence for ADP-Pi-F-actin as the major intermediate in ATP-actin polymerization: rate of dissociation of Pi from actin filaments. Biochemistry 1986, 25:7789-7792.
    • (1986) Biochemistry , vol.25 , pp. 7789-7792
    • Carlier, M.F.1    Pantaloni, D.2
  • 30
    • 0037138384 scopus 로고    scopus 로고
    • WH2 domain: a small, versatile adapter for actin monomers
    • Paunola E., Mattila P.K., Lappalainen P. WH2 domain: a small, versatile adapter for actin monomers. FEBS Lett. 2002, 513:92-97.
    • (2002) FEBS Lett. , vol.513 , pp. 92-97
    • Paunola, E.1    Mattila, P.K.2    Lappalainen, P.3
  • 31
    • 35348969696 scopus 로고    scopus 로고
    • The beta-thymosin/WH2 fold: multifunctionality and structure
    • Dominguez R. The beta-thymosin/WH2 fold: multifunctionality and structure. Ann. NY Acad. Sci. 2007, 1112:86-94.
    • (2007) Ann. NY Acad. Sci. , vol.1112 , pp. 86-94
    • Dominguez, R.1
  • 33
    • 0025355476 scopus 로고
    • Isolation of a 5-kilodalton actin-sequestering peptide from human blood platelets
    • Safer D., Golla R., Nachmias V.T. Isolation of a 5-kilodalton actin-sequestering peptide from human blood platelets. Proc. Natl. Acad. Sci. USA 1990, 87:2536-2540.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 2536-2540
    • Safer, D.1    Golla, R.2    Nachmias, V.T.3
  • 35
    • 0021766640 scopus 로고
    • Quantitative analysis of the effect of Acanthamoeba profilin on actin filament nucleation and elongation
    • Pollard T.D., Cooper J.A. Quantitative analysis of the effect of Acanthamoeba profilin on actin filament nucleation and elongation. Biochemistry 1984, 23:6631-6641.
    • (1984) Biochemistry , vol.23 , pp. 6631-6641
    • Pollard, T.D.1    Cooper, J.A.2
  • 36
    • 0028136434 scopus 로고
    • Purification of a cortical complex containing two unconventional actins from Acanthamoeba by affinity chromatography on profilin-agarose
    • Machesky L.M., Atkinson S.J., Ampe C., Vandekerckhove J., Pollard T.D. Purification of a cortical complex containing two unconventional actins from Acanthamoeba by affinity chromatography on profilin-agarose. J. Cell Biol. 1994, 127:107-115.
    • (1994) J. Cell Biol. , vol.127 , pp. 107-115
    • Machesky, L.M.1    Atkinson, S.J.2    Ampe, C.3    Vandekerckhove, J.4    Pollard, T.D.5
  • 37
    • 0032479578 scopus 로고    scopus 로고
    • Interaction of human Arp2/3 complex and the Listeria monocytogenes ActA protein in actin filament nucleation
    • Welch M.D., Rosenblatt J., Skoble J., Portnoy D.A., Mitchison T.J. Interaction of human Arp2/3 complex and the Listeria monocytogenes ActA protein in actin filament nucleation. Science 1998, 281:105-108.
    • (1998) Science , vol.281 , pp. 105-108
    • Welch, M.D.1    Rosenblatt, J.2    Skoble, J.3    Portnoy, D.A.4    Mitchison, T.J.5
  • 38
    • 0032585538 scopus 로고    scopus 로고
    • Scar1 and the related Wiskott-Aldrich syndrome protein, WASP, regulate the actin cytoskeleton through the Arp2/3 complex
    • Machesky L.M., Insall R.H. Scar1 and the related Wiskott-Aldrich syndrome protein, WASP, regulate the actin cytoskeleton through the Arp2/3 complex. Curr. Biol. 1998, 8:1347-1356.
    • (1998) Curr. Biol. , vol.8 , pp. 1347-1356
    • Machesky, L.M.1    Insall, R.H.2
  • 40
    • 0033574722 scopus 로고    scopus 로고
    • The interaction between N-WASP and the Arp2/3 complex links Cdc42-dependent signals to actin assembly
    • Rohatgi R., Ma L., Miki H., Lopez M., Kirchhausen T., Takenawa T., Kirschner M.W. The interaction between N-WASP and the Arp2/3 complex links Cdc42-dependent signals to actin assembly. Cell 1999, 97:221-231.
    • (1999) Cell , vol.97 , pp. 221-231
    • Rohatgi, R.1    Ma, L.2    Miki, H.3    Lopez, M.4    Kirchhausen, T.5    Takenawa, T.6    Kirschner, M.W.7
  • 41
    • 0033528995 scopus 로고    scopus 로고
    • Activation of the yeast Arp2/3 complex by Bee1p, a WASP-family protein
    • Winter D., Lechler T., Li R. Activation of the yeast Arp2/3 complex by Bee1p, a WASP-family protein. Curr. Biol. 1999, 9:501-504.
    • (1999) Curr. Biol. , vol.9 , pp. 501-504
    • Winter, D.1    Lechler, T.2    Li, R.3
  • 42
    • 0033587188 scopus 로고    scopus 로고
    • The Wiskott-Aldrich syndrome protein directs actin-based motility by stimulating actin nucleation with the Arp2/3 complex
    • Yarar D., To W., Abo A., Welch D.D. The Wiskott-Aldrich syndrome protein directs actin-based motility by stimulating actin nucleation with the Arp2/3 complex. Curr. Biol. 1999, 9:555-558.
    • (1999) Curr. Biol. , vol.9 , pp. 555-558
    • Yarar, D.1    To, W.2    Abo, A.3    Welch, D.D.4
  • 48
    • 34147144059 scopus 로고    scopus 로고
    • A type III secretion system in Vibrio cholerae translocates a formin/Spire hybrid-like actin nucleator to promote intestinal colonization
    • Tam V.C., Serruto D., Dziejman M., Brieher W., Mekalanos J.J. A type III secretion system in Vibrio cholerae translocates a formin/Spire hybrid-like actin nucleator to promote intestinal colonization. Cell Host Microbe 2007, 1:95-107.
    • (2007) Cell Host Microbe , vol.1 , pp. 95-107
    • Tam, V.C.1    Serruto, D.2    Dziejman, M.3    Brieher, W.4    Mekalanos, J.J.5
  • 52
    • 78149285594 scopus 로고    scopus 로고
    • Rickettsia Sca2 is a bacterial formin-like mediator of actin-based motility
    • Haglund C.M., Choe J.E., Skau C.T., Kovar D.R., Welch M.D. Rickettsia Sca2 is a bacterial formin-like mediator of actin-based motility. Nat. Cell Biol. 2010, 12:1057-1063.
    • (2010) Nat. Cell Biol. , vol.12 , pp. 1057-1063
    • Haglund, C.M.1    Choe, J.E.2    Skau, C.T.3    Kovar, D.R.4    Welch, M.D.5
  • 54
    • 58749091822 scopus 로고    scopus 로고
    • The nature of the globular- to fibrous-actin transition
    • Oda T., Iwasa M., Aihara T., Maeda 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    Maeda, Y.4    Narita, A.5
  • 55
    • 58749101334 scopus 로고    scopus 로고
    • Structural biology: actin in a twist
    • Holmes K.C. Structural biology: actin in a twist. Nature 2009, 457:389-390.
    • (2009) Nature , vol.457 , pp. 389-390
    • Holmes, K.C.1
  • 57
    • 19544386803 scopus 로고    scopus 로고
    • Structural and mechanistic insights into the interaction between Rho and mammalian Dia
    • Rose R., Weyand M., Lammers M., Ishizaki T., Ahmadian M.R., Wittinghofer A. Structural and mechanistic insights into the interaction between Rho and mammalian Dia. Nature 2005, 435:513-518.
    • (2005) Nature , vol.435 , pp. 513-518
    • Rose, R.1    Weyand, M.2    Lammers, M.3    Ishizaki, T.4    Ahmadian, M.R.5    Wittinghofer, A.6
  • 58
    • 28644442126 scopus 로고    scopus 로고
    • The regulation of mDia1 by autoinhibition and its release by Rho•GTP
    • Lammers M., Rose R., Scrima A., Wittinghofer A. The regulation of mDia1 by autoinhibition and its release by Rho•GTP. EMBO J. 2005, 24:4176-4187.
    • (2005) EMBO J. , vol.24 , pp. 4176-4187
    • Lammers, M.1    Rose, R.2    Scrima, A.3    Wittinghofer, A.4
  • 59
    • 13444280218 scopus 로고    scopus 로고
    • Structural basis of actin filament nucleation and processive capping by a formin homology 2 domain
    • Otomo T., Tomchick D.R., Otomo C., Panchal S.C., Machius M., Rosen M.K. Structural basis of actin filament nucleation and processive capping by a formin homology 2 domain. Nature 2005, 433:488-494.
    • (2005) Nature , vol.433 , pp. 488-494
    • Otomo, T.1    Tomchick, D.R.2    Otomo, C.3    Panchal, S.C.4    Machius, M.5    Rosen, M.K.6
  • 61
    • 1542269073 scopus 로고    scopus 로고
    • Crystal structures of a formin homology-2 domain reveal a tethered dimer architecture
    • Xu Y., Moseley J.B., Sagot I., Poy F., Pellman D., Goode B.L., Eck M.J. Crystal structures of a formin homology-2 domain reveal a tethered dimer architecture. Cell 2004, 116:711-723.
    • (2004) Cell , vol.116 , 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
  • 62
    • 1642391823 scopus 로고    scopus 로고
    • Formin-induced nucleation of actin filaments
    • Zigmond S.H. Formin-induced nucleation of actin filaments. Curr. Opin. Cell Biol. 2004, 16:99-105.
    • (2004) Curr. Opin. Cell Biol. , vol.16 , pp. 99-105
    • Zigmond, S.H.1
  • 63
    • 0028053435 scopus 로고
    • Diaphanous is required for cytokinesis in Drosophila and shares domains of similarity with the products of the limb deformity gene
    • Castrillon D.H., Wasserman S.A. Diaphanous is required for cytokinesis in Drosophila and shares domains of similarity with the products of the limb deformity gene. Development 1994, 120:3367-3377.
    • (1994) Development , vol.120 , pp. 3367-3377
    • Castrillon, D.H.1    Wasserman, S.A.2
  • 64
    • 0033160196 scopus 로고    scopus 로고
    • Cooperation between mDia1 and ROCK in Rho-induced actin reorganization
    • Watanabe N., Kato T., Fujita A., Ishizaki T., Narumiya S. Cooperation between mDia1 and ROCK in Rho-induced actin reorganization. Nat. Cell Biol. 1999, 1:136-143.
    • (1999) Nat. Cell Biol. , vol.1 , pp. 136-143
    • Watanabe, N.1    Kato, T.2    Fujita, A.3    Ishizaki, T.4    Narumiya, S.5
  • 66
    • 40149105917 scopus 로고    scopus 로고
    • The role of the FH1 domain and profilin in formin-mediated actin-filament elongation and nucleation
    • Paul A.S., Pollard T.D. The role of the FH1 domain and profilin in formin-mediated actin-filament elongation and nucleation. Curr. Biol. 2008, 18:9-19.
    • (2008) Curr. Biol. , vol.18 , pp. 9-19
    • Paul, A.S.1    Pollard, T.D.2
  • 67
    • 31044433924 scopus 로고    scopus 로고
    • Control of the assembly of ATP- and ADP-actin by formins and profilin
    • Kovar D.R., Harris E.S., Mahaffy R., Higgs H.N., Pollard T.D. Control of the assembly of ATP- and ADP-actin by formins and profilin. Cell 2006, 124:423-435.
    • (2006) Cell , vol.124 , pp. 423-435
    • Kovar, D.R.1    Harris, E.S.2    Mahaffy, R.3    Higgs, H.N.4    Pollard, T.D.5
  • 68
    • 78650988290 scopus 로고    scopus 로고
    • Rotational movement of the formin mDia1 along the double helical strand of an actin filament
    • Mizuno H., Higashida C., Yuan Y., Ishizaki T., Narumiya S., Watanabe N. Rotational movement of the formin mDia1 along the double helical strand of an actin filament. Science 2011, 331:80-83.
    • (2011) Science , vol.331 , pp. 80-83
    • Mizuno, H.1    Higashida, C.2    Yuan, Y.3    Ishizaki, T.4    Narumiya, S.5    Watanabe, N.6
  • 69
    • 28044470753 scopus 로고    scopus 로고
    • Actin-bound structures of Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 and the implications for filament assembly
    • Chereau D., Kerff F., Graceffa P., Grabarek Z., Langsetmo K., Dominguez R. Actin-bound structures of Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 and the implications for filament assembly. Proc. Natl. Acad. Sci. USA 2005, 102:16644-16649.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 16644-16649
    • Chereau, D.1    Kerff, F.2    Graceffa, P.3    Grabarek, Z.4    Langsetmo, K.5    Dominguez, R.6
  • 70
    • 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
  • 71
    • 77957267062 scopus 로고    scopus 로고
    • Structure of a longitudinal actin dimer assembled by tandem W domains: implications for actin filament nucleation
    • Rebowski G., Namgoong S., Boczkowska M., Leavis P.C., Navaza J., Dominguez R. Structure of a longitudinal actin dimer assembled by tandem W domains: implications for actin filament nucleation. J. Mol. Biol. 2010, 403:11-23.
    • (2010) J. Mol. Biol. , vol.403 , pp. 11-23
    • Rebowski, G.1    Namgoong, S.2    Boczkowska, M.3    Leavis, P.C.4    Navaza, J.5    Dominguez, R.6
  • 73
    • 34247619703 scopus 로고    scopus 로고
    • Insights into the influence of nucleotides on actin family proteins from seven structures of Arp2/3 complex
    • Nolen B.J., Pollard T.D. Insights into the influence of nucleotides on actin family proteins from seven structures of Arp2/3 complex. Mol. Cell 2007, 26:449-457.
    • (2007) Mol. Cell , vol.26 , pp. 449-457
    • Nolen, B.J.1    Pollard, T.D.2
  • 75
    • 33744514937 scopus 로고    scopus 로고
    • Actin binding to the central domain of WASP/Scar proteins plays a critical role in the activation of the Arp2/3 complex
    • Kelly A.E., Kranitz H., Dotsch V., Mullins R.D. Actin binding to the central domain of WASP/Scar proteins plays a critical role in the activation of the Arp2/3 complex. J. Biol. Chem. 2006, 281:10589-10597.
    • (2006) J. Biol. Chem. , vol.281 , pp. 10589-10597
    • Kelly, A.E.1    Kranitz, H.2    Dotsch, V.3    Mullins, R.D.4
  • 76
    • 0035793587 scopus 로고    scopus 로고
    • Activation of the Arp2/3 complex by the Listeria acta protein: acta binds two actin monomers and three subunits of the Arp2/3 complex
    • Zalevsky J., Grigorova I., Mullins R.D. Activation of the Arp2/3 complex by the Listeria acta protein: acta binds two actin monomers and three subunits of the Arp2/3 complex. J. Biol. Chem. 2001, 276:3468-3475.
    • (2001) J. Biol. Chem. , vol.276 , pp. 3468-3475
    • Zalevsky, J.1    Grigorova, I.2    Mullins, R.D.3
  • 79
    • 0141809370 scopus 로고    scopus 로고
    • Tropomodulin contains two actin filament pointed end-capping domains
    • Fowler V.M., Greenfield N.J., Moyer J. Tropomodulin contains two actin filament pointed end-capping domains. J. Biol. Chem. 2003, 278:40000-40009.
    • (2003) J. Biol. Chem. , vol.278 , pp. 40000-40009
    • Fowler, V.M.1    Greenfield, N.J.2    Moyer, J.3
  • 80
    • 0036841312 scopus 로고    scopus 로고
    • Crystal structure of the C-terminal half of tropomodulin and structural basis of actin filament pointed-end capping
    • Krieger I., Kostyukova A., Yamashita A., Nitanai Y., Maeda Y. Crystal structure of the C-terminal half of tropomodulin and structural basis of actin filament pointed-end capping. Biophys. J. 2002, 83:2716-2725.
    • (2002) Biophys. J. , vol.83 , pp. 2716-2725
    • Krieger, I.1    Kostyukova, A.2    Yamashita, A.3    Nitanai, Y.4    Maeda, Y.5
  • 81
    • 0033553508 scopus 로고    scopus 로고
    • Structure of the enabled/VASP homology 1 domain-peptide complex: a key component in the spatial control of actin assembly
    • Prehoda K.E., Lee D.J., Lim W.A. Structure of the enabled/VASP homology 1 domain-peptide complex: a key component in the spatial control of actin assembly. Cell 1999, 97:471-480.
    • (1999) Cell , vol.97 , pp. 471-480
    • Prehoda, K.E.1    Lee, D.J.2    Lim, W.A.3
  • 82
    • 35649021883 scopus 로고    scopus 로고
    • Structural basis for the recruitment of profilin-actin complexes during filament elongation by Ena/VASP
    • Ferron F., Rebowski G., Lee S.H., Dominguez R. Structural basis for the recruitment of profilin-actin complexes during filament elongation by Ena/VASP. EMBO J. 2007, 26:4597-4606.
    • (2007) EMBO J. , vol.26 , pp. 4597-4606
    • Ferron, F.1    Rebowski, G.2    Lee, S.H.3    Dominguez, R.4
  • 84
    • 0029157584 scopus 로고
    • Identification, purification, and characterization of a zyxin-related protein that binds the focal adhesion and microfilament protein VASP (vasodilator-stimulated phosphoprotein)
    • Reinhard M., Jouvenal K., Tripier D., Walter U. Identification, purification, and characterization of a zyxin-related protein that binds the focal adhesion and microfilament protein VASP (vasodilator-stimulated phosphoprotein). Proc. Natl. Acad. Sci. USA 1995, 92:7956-7960.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 7956-7960
    • Reinhard, M.1    Jouvenal, K.2    Tripier, D.3    Walter, U.4
  • 85
    • 0029761645 scopus 로고    scopus 로고
    • The focal-adhesion vasodilator-stimulated phosphoprotein (VASP) binds to the proline-rich domain in vinculin
    • Brindle N.P., Holt M.R., Davies J.E., Price C.J., Critchley D.R. The focal-adhesion vasodilator-stimulated phosphoprotein (VASP) binds to the proline-rich domain in vinculin. Biochem. J. 1996, 318(Pt 3):753-757.
    • (1996) Biochem. J. , vol.318 , Issue.PT 3 , pp. 753-757
    • Brindle, N.P.1    Holt, M.R.2    Davies, J.E.3    Price, C.J.4    Critchley, D.R.5
  • 86
    • 0030577348 scopus 로고    scopus 로고
    • VASP interaction with vinculin: a recurring theme of interactions with proline-rich motifs
    • Reinhard M., Rudiger M., Jockusch B.M., Walter U. VASP interaction with vinculin: a recurring theme of interactions with proline-rich motifs. FEBS Lett. 1996, 399:103-107.
    • (1996) FEBS Lett. , vol.399 , pp. 103-107
    • Reinhard, M.1    Rudiger, M.2    Jockusch, B.M.3    Walter, U.4
  • 88
    • 33744951973 scopus 로고    scopus 로고
    • Migfilin interacts with vasodilator-stimulated phosphoprotein (VASP) and regulates VASP localization to cell-matrix adhesions and migration
    • Zhang Y., Tu Y., Gkretsi V., Wu C. Migfilin interacts with vasodilator-stimulated phosphoprotein (VASP) and regulates VASP localization to cell-matrix adhesions and migration. J. Biol. Chem. 2006, 281:12397-12407.
    • (2006) J. Biol. Chem. , vol.281 , pp. 12397-12407
    • Zhang, Y.1    Tu, Y.2    Gkretsi, V.3    Wu, C.4
  • 91
    • 0037177848 scopus 로고    scopus 로고
    • Control of actin dynamics by proteins made of beta-thymosin repeats: the actobindin family
    • Hertzog M., Yarmola E.G., Didry D., Bubb M.R., Carlier M.F. Control of actin dynamics by proteins made of beta-thymosin repeats: the actobindin family. J. Biol. Chem. 2002, 277:14786-14792.
    • (2002) J. Biol. Chem. , vol.277 , pp. 14786-14792
    • Hertzog, M.1    Yarmola, E.G.2    Didry, D.3    Bubb, M.R.4    Carlier, M.F.5
  • 93
    • 4644284610 scopus 로고    scopus 로고
    • Tetrathymosin-beta is required for actin dynamics in Caenorhabditis elegans and acts via functionally different actin-binding repeats
    • Van Troys M., Ono K., Dewitte D., Jonckheere V., De Ruyck N., Vandekerckhove J., Ono S., Ampe C. Tetrathymosin-beta is required for actin dynamics in Caenorhabditis elegans and acts via functionally different actin-binding repeats. Mol. Biol. Cell. 2004, 15:4735-4748.
    • (2004) Mol. Biol. Cell. , vol.15 , pp. 4735-4748
    • Van Troys, M.1    Ono, K.2    Dewitte, D.3    Jonckheere, V.4    De Ruyck, N.5    Vandekerckhove, J.6    Ono, S.7    Ampe, C.8
  • 95
    • 0024723365 scopus 로고
    • Cappuccino and Spire: two unique maternal-effect loci required for both the anteroposterior and dorsoventral patterns of the Drosophila embryo
    • Manseau L.J., Schupbach T. Cappuccino and Spire: two unique maternal-effect loci required for both the anteroposterior and dorsoventral patterns of the Drosophila embryo. Genes Dev. 1989, 3:1437-1452.
    • (1989) Genes Dev. , vol.3 , pp. 1437-1452
    • Manseau, L.J.1    Schupbach, T.2
  • 96
    • 34848873760 scopus 로고    scopus 로고
    • Capu and Spire assemble a cytoplasmic actin mesh that maintains microtubule organization in the Drosophila oocyte
    • Dahlgaard K., Raposo A.A., Niccoli T., Johnston D. Capu and Spire assemble a cytoplasmic actin mesh that maintains microtubule organization in the Drosophila oocyte. Dev. Cell. 2007, 13:539-553.
    • (2007) Dev. Cell. , vol.13 , pp. 539-553
    • Dahlgaard, K.1    Raposo, A.A.2    Niccoli, T.3    Johnston, D.4
  • 98
    • 69949127688 scopus 로고    scopus 로고
    • Identification of a short Spir interaction sequence at the C-terminal end of formin subgroup proteins
    • Pechlivanis M., Samol A., Kerkhoff E. Identification of a short Spir interaction sequence at the C-terminal end of formin subgroup proteins. J. Biol. Chem. 2009, 284:25324-25333.
    • (2009) J. Biol. Chem. , vol.284 , pp. 25324-25333
    • Pechlivanis, M.1    Samol, A.2    Kerkhoff, E.3
  • 99
    • 1642400437 scopus 로고    scopus 로고
    • Overlapping expression pattern of the actin organizers Spir-1 and formin-2 in the developing mouse nervous system and the adult brain
    • Schumacher N., Borawski J.M., Leberfinger C.B., Gessler M., Kerkhoff E. Overlapping expression pattern of the actin organizers Spir-1 and formin-2 in the developing mouse nervous system and the adult brain. Gene Expr. Patterns 2004, 4:249-255.
    • (2004) Gene Expr. Patterns , vol.4 , pp. 249-255
    • Schumacher, N.1    Borawski, J.M.2    Leberfinger, C.B.3    Gessler, M.4    Kerkhoff, E.5
  • 104
    • 79251473104 scopus 로고    scopus 로고
    • Actin motility: formin a SCAry tail
    • Alberts A., Way M. Actin motility: formin a SCAry tail. Curr. Biol. 2011, 21:R27-R30.
    • (2011) Curr. Biol. , vol.21
    • Alberts, A.1    Way, M.2
  • 105
    • 77951232931 scopus 로고    scopus 로고
    • Disruption of the Rickettsia rickettsii Sca2 autotransporter inhibits actin-based motility
    • Kleba B., Clark T.R., Lutter E.I., Ellison D.W., Hackstadt T. Disruption of the Rickettsia rickettsii Sca2 autotransporter inhibits actin-based motility. Infect. Immunol. 2010, 78:2240-2247.
    • (2010) Infect. Immunol. , vol.78 , pp. 2240-2247
    • Kleba, B.1    Clark, T.R.2    Lutter, E.I.3    Ellison, D.W.4    Hackstadt, T.5
  • 109
    • 0032568650 scopus 로고    scopus 로고
    • The interaction of Arp2/3 complex with actin: nucleation, high affinity pointed end capping, and formation of branching networks of filaments
    • Mullins R.D., Heuser J.A., Pollard T.D. The interaction of Arp2/3 complex with actin: nucleation, high affinity pointed end capping, and formation of branching networks of filaments. Proc. Natl. Acad. Sci. USA 1998, 95:6181-6186.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 6181-6186
    • Mullins, R.D.1    Heuser, J.A.2    Pollard, T.D.3
  • 111
    • 46149096223 scopus 로고    scopus 로고
    • WHAMM is an Arp2/3 complex activator that binds microtubules and functions in ER to Golgi transport
    • Campellone K.G., Webb N.J., Znameroski E.A., Welch M.D. WHAMM is an Arp2/3 complex activator that binds microtubules and functions in ER to Golgi transport. Cell 2008, 134:148-161.
    • (2008) Cell , vol.134 , pp. 148-161
    • Campellone, K.G.1    Webb, N.J.2    Znameroski, E.A.3    Welch, M.D.4
  • 113
    • 0032430263 scopus 로고    scopus 로고
    • The Arp2/3 complex mediates actin polymerization induced by the small GTP-binding protein Cdc42
    • Ma L., Rohatgi R., Kirschner M.W. The Arp2/3 complex mediates actin polymerization induced by the small GTP-binding protein Cdc42. Proc. Natl. Acad. Sci. USA 1998, 95:15362-15367.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 15362-15367
    • Ma, L.1    Rohatgi, R.2    Kirschner, M.W.3
  • 115
    • 0034624753 scopus 로고    scopus 로고
    • Autoinhibition and activation mechanisms of the Wiskott-Aldrich syndrome protein
    • Kim A.S., Kakalis L.T., Abdul-Manan N., Liu G.A., Rosen M.K. Autoinhibition and activation mechanisms of the Wiskott-Aldrich syndrome protein. Nature 2000, 404:151-158.
    • (2000) Nature , vol.404 , pp. 151-158
    • Kim, A.S.1    Kakalis, L.T.2    Abdul-Manan, N.3    Liu, G.A.4    Rosen, M.K.5
  • 116
    • 0037102301 scopus 로고    scopus 로고
    • Mechanism of regulation of WAVE1-induced actin nucleation by Rac1 and Nck
    • Eden S., Rohatgi R., Podtelejnikov A.V., Mann M., Kirschner M.W. Mechanism of regulation of WAVE1-induced actin nucleation by Rac1 and Nck. Nature 2002, 418:790-793.
    • (2002) Nature , vol.418 , pp. 790-793
    • Eden, S.1    Rohatgi, R.2    Podtelejnikov, A.V.3    Mann, M.4    Kirschner, M.W.5
  • 117
    • 4644342865 scopus 로고    scopus 로고
    • Regulation of WASP/WAVE proteins: making a long story short
    • Bompard G., Caron E. Regulation of WASP/WAVE proteins: making a long story short. J. Cell Biol. 2004, 166:957-962.
    • (2004) J. Cell Biol. , vol.166 , pp. 957-962
    • Bompard, G.1    Caron, E.2
  • 118
    • 0034721696 scopus 로고    scopus 로고
    • Integration of multiple signals through cooperative regulation of the N-WASP-Arp2/3 complex
    • Prehoda K.E., Scott J.A., Mullins R.D., Lim W.A. Integration of multiple signals through cooperative regulation of the N-WASP-Arp2/3 complex. Science 2000, 290:801-806.
    • (2000) Science , vol.290 , pp. 801-806
    • Prehoda, K.E.1    Scott, J.A.2    Mullins, R.D.3    Lim, W.A.4
  • 119
    • 70449112591 scopus 로고    scopus 로고
    • Activation of the WAVE complex by coincident signals controls actin assembly
    • Lebensohn A.M., Kirschner M.W. Activation of the WAVE complex by coincident signals controls actin assembly. Mol. Cell. 2009, 36:512-524.
    • (2009) Mol. Cell. , vol.36 , pp. 512-524
    • Lebensohn, A.M.1    Kirschner, M.W.2
  • 120
    • 22144490590 scopus 로고    scopus 로고
    • Inclusion of Scar/WAVE3 in a similar complex to Scar/WAVE1 and 2
    • Stovold C.F., Millard T.H., Machesky L.M. Inclusion of Scar/WAVE3 in a similar complex to Scar/WAVE1 and 2. BMC Cell Biol. 2005, 6:11.
    • (2005) BMC Cell Biol. , vol.6 , pp. 11
    • Stovold, C.F.1    Millard, T.H.2    Machesky, L.M.3
  • 124
    • 53449100875 scopus 로고    scopus 로고
    • Actin cytoskeletal dynamics in smooth muscle: a new paradigm for the regulation of smooth muscle contraction
    • Gunst S.J., Zhang W. Actin cytoskeletal dynamics in smooth muscle: a new paradigm for the regulation of smooth muscle contraction. Am. J. Physiol. Cell. Physiol. 2008, 295:C576-C587.
    • (2008) Am. J. Physiol. Cell. Physiol. , vol.295
    • Gunst, S.J.1    Zhang, W.2
  • 125
    • 80051977000 scopus 로고    scopus 로고
    • Structural and biochemical characterization of two binding sites for nucleation-promoting factor WASp-VCA on Arp2/3 complex. Proc
    • Ti S.C., Jurgenson C.T., Nolen B.J., Pollard T.D. Structural and biochemical characterization of two binding sites for nucleation-promoting factor WASp-VCA on Arp2/3 complex. Proc. Natl. Acad. Sci. USA 2011, 108:E463-E471.
    • (2011) Natl. Acad. Sci. USA , vol.108
    • Ti, S.C.1    Jurgenson, C.T.2    Nolen, B.J.3    Pollard, T.D.4
  • 128
    • 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. Signaling 2008, 1:pe37.
    • (2008) Sci. Signaling , vol.1
    • Sanger, J.M.1    Sanger, J.W.2
  • 129
  • 130
    • 0142157493 scopus 로고    scopus 로고
    • Tropomodulins: life at the slow end
    • Fischer R.S., Fowler V.M. Tropomodulins: life at the slow end. Trends Cell. Biol. 2003, 13:593-601.
    • (2003) Trends Cell. Biol. , vol.13 , pp. 593-601
    • Fischer, R.S.1    Fowler, V.M.2
  • 131
    • 34548176712 scopus 로고    scopus 로고
    • Molecular basis of tropomyosin binding to tropomodulin, an actin-capping protein
    • Kostyukova A.S., Hitchcock-Degregori S.E., Greenfield N.J. Molecular basis of tropomyosin binding to tropomodulin, an actin-capping protein. J. Mol. Biol. 2007, 372:608-618.
    • (2007) J. Mol. Biol. , vol.372 , pp. 608-618
    • Kostyukova, A.S.1    Hitchcock-Degregori, S.E.2    Greenfield, N.J.3
  • 132
    • 62449145371 scopus 로고    scopus 로고
    • Gestalt-binding of tropomyosin to actin filaments
    • Holmes K.C., Lehman W. Gestalt-binding of tropomyosin to actin filaments. J. Muscle Res. Cell. Motil. 2008, 29:213-219.
    • (2008) J. Muscle Res. Cell. Motil. , vol.29 , pp. 213-219
    • Holmes, K.C.1    Lehman, W.2
  • 133
    • 79951821838 scopus 로고    scopus 로고
    • Tropomyosin: the gatekeeper's view of the actin filament revealed
    • Dominguez R. Tropomyosin: the gatekeeper's view of the actin filament revealed. Biophys. J. 2011, 100:797-798.
    • (2011) Biophys. J. , vol.100 , pp. 797-798
    • Dominguez, R.1
  • 134
    • 3142773420 scopus 로고    scopus 로고
    • Cytoplasmic nuclear transfer of the actin-capping protein tropomodulin
    • Kong K.Y., Kedes L. Cytoplasmic nuclear transfer of the actin-capping protein tropomodulin. J. Biol. Chem. 2004, 279:30856-30864.
    • (2004) J. Biol. Chem. , vol.279 , pp. 30856-30864
    • Kong, K.Y.1    Kedes, L.2
  • 136
    • 68949183227 scopus 로고    scopus 로고
    • Ena/VASP: towards resolving a pointed controversy at the barbed end
    • Bear J.E., Gertler F.B. Ena/VASP: towards resolving a pointed controversy at the barbed end. J. Cell Sci. 2009, 122:1947-1953.
    • (2009) J. Cell Sci. , vol.122 , pp. 1947-1953
    • Bear, J.E.1    Gertler, F.B.2
  • 141
    • 46549086642 scopus 로고    scopus 로고
    • Ena/VASP: proteins at the tip of the nervous system
    • Drees F., Gertler F.B. Ena/VASP: proteins at the tip of the nervous system. Curr. Opin. Neurobiol. 2008, 18:53-59.
    • (2008) Curr. Opin. Neurobiol. , vol.18 , pp. 53-59
    • Drees, F.1    Gertler, F.B.2
  • 142
    • 33748745132 scopus 로고    scopus 로고
    • INF2 is a WASP homology 2 motif-containing formin that severs actin filaments and accelerates both polymerization and depolymerization
    • Chhabra E.S., Higgs H.N. INF2 is a WASP homology 2 motif-containing formin that severs actin filaments and accelerates both polymerization and depolymerization. J. Biol. Chem. 2006, 281:26754-26767.
    • (2006) J. Biol. Chem. , vol.281 , pp. 26754-26767
    • Chhabra, E.S.1    Higgs, H.N.2
  • 143
    • 67650566835 scopus 로고    scopus 로고
    • INF2 is an endoplasmic reticulum-associated formin protein
    • Chhabra E.S., Ramabhadran V., Gerber S.A., Higgs H.N. INF2 is an endoplasmic reticulum-associated formin protein. J. Cell Sci. 2009, 122:1430-1440.
    • (2009) J. Cell Sci. , vol.122 , pp. 1430-1440
    • Chhabra, E.S.1    Ramabhadran, V.2    Gerber, S.A.3    Higgs, H.N.4
  • 144
    • 0033551783 scopus 로고    scopus 로고
    • The EVH2 domain of the vasodilator-stimulated phosphoprotein mediates tetramerization, F-actin binding, and actin bundle formation
    • Bachmann C., Fischer L., Walter U., Reinhard M. The EVH2 domain of the vasodilator-stimulated phosphoprotein mediates tetramerization, F-actin binding, and actin bundle formation. J. Biol. Chem. 1999, 274:23549-23557.
    • (1999) J. Biol. Chem. , vol.274 , pp. 23549-23557
    • Bachmann, C.1    Fischer, L.2    Walter, U.3    Reinhard, M.4
  • 145
    • 0013033597 scopus 로고    scopus 로고
    • The structure and function of proline recognition domains
    • Zarrinpar A., Bhattacharyya R.P., Lim W.A. The structure and function of proline recognition domains. Sci. STKE 2003, 2003:RE8.
    • (2003) Sci. STKE , vol.2003
    • Zarrinpar, A.1    Bhattacharyya, R.P.2    Lim, W.A.3
  • 146
    • 0030851599 scopus 로고    scopus 로고
    • Profilin interacts with the Gly-Pro-Pro-Pro-Pro-Pro sequences of vasodilator-stimulated phosphoprotein (VASP): implications for actin-based Listeria motility
    • Kang F., Laine R.O., Bubb M.R., Southwick F.S., Purich D.L. Profilin interacts with the Gly-Pro-Pro-Pro-Pro-Pro sequences of vasodilator-stimulated phosphoprotein (VASP): implications for actin-based Listeria motility. Biochemistry 1997, 36:8384-8392.
    • (1997) Biochemistry , vol.36 , pp. 8384-8392
    • Kang, F.1    Laine, R.O.2    Bubb, M.R.3    Southwick, F.S.4    Purich, D.L.5
  • 147
    • 0034097554 scopus 로고    scopus 로고
    • Accumulation of profilin II at the surface of Listeria is concomitant with the onset of motility and correlates with bacterial speed
    • Geese M., Schluter K., Rothkegel M., Jockusch B.M., Wehland J., Sechi A.S. Accumulation of profilin II at the surface of Listeria is concomitant with the onset of motility and correlates with bacterial speed. J. Cell Sci. 2000, 113(Pt 8):1415-1426.
    • (2000) J. Cell Sci. , vol.113 , Issue.PT 8 , pp. 1415-1426
    • Geese, M.1    Schluter, K.2    Rothkegel, M.3    Jockusch, B.M.4    Wehland, J.5    Sechi, A.S.6
  • 148
    • 0036402424 scopus 로고    scopus 로고
    • A direct-transfer polymerization model explains how the multiple profilin-binding sites in the actoclampin motor promote rapid actin-based motility
    • Dickinson R.B., Southwick F.S., Purich D.L. A direct-transfer polymerization model explains how the multiple profilin-binding sites in the actoclampin motor promote rapid actin-based motility. Arch. Biochem. Biophys. 2002, 406:296-301.
    • (2002) Arch. Biochem. Biophys. , vol.406 , pp. 296-301
    • Dickinson, R.B.1    Southwick, F.S.2    Purich, D.L.3
  • 149
    • 0035955727 scopus 로고    scopus 로고
    • ActA from Listeria monocytogenes can interact with up to four Ena/VASP homology 1 domains simultaneously
    • Machner M.P., Urbanke C., Barzik M., Otten S., Sechi A.S., Wehland J., Heinz D.W. ActA from Listeria monocytogenes can interact with up to four Ena/VASP homology 1 domains simultaneously. J. Biol. Chem. 2001, 276:40096-40103.
    • (2001) J. Biol. Chem. , vol.276 , pp. 40096-40103
    • Machner, M.P.1    Urbanke, C.2    Barzik, M.3    Otten, S.4    Sechi, A.S.5    Wehland, J.6    Heinz, D.W.7
  • 150
    • 0037482886 scopus 로고    scopus 로고
    • A crucial role for profilin-actin in the intracellular motility of Listeria monocytogenes
    • Grenklo S., Geese M., Lindberg U., Wehland J., Karlsson R., Sechi A.S. A crucial role for profilin-actin in the intracellular motility of Listeria monocytogenes. EMBO Rep. 2003, 4:523-529.
    • (2003) EMBO Rep. , vol.4 , pp. 523-529
    • Grenklo, S.1    Geese, M.2    Lindberg, U.3    Wehland, J.4    Karlsson, R.5    Sechi, A.S.6
  • 151
    • 0141677821 scopus 로고    scopus 로고
    • Ena/VASP proteins contribute to Listeria monocytogenes pathogenesis by controlling temporal and spatial persistence of bacterial actin-based motility
    • Auerbuch V., Loureiro J.J., Gertler F.B., Theriot J.A., Portnoy D.A. Ena/VASP proteins contribute to Listeria monocytogenes pathogenesis by controlling temporal and spatial persistence of bacterial actin-based motility. Mol. Microbiol. 2003, 49:1361-1375.
    • (2003) Mol. Microbiol. , vol.49 , pp. 1361-1375
    • Auerbuch, V.1    Loureiro, J.J.2    Gertler, F.B.3    Theriot, J.A.4    Portnoy, D.A.5
  • 153
    • 44349090393 scopus 로고    scopus 로고
    • Ena/VASP proteins capture actin filament barbed ends
    • Pasic L., Kotova T., Schafer D.A. Ena/VASP proteins capture actin filament barbed ends. J. Biol. Chem. 2008, 283:9814-9819.
    • (2008) J. Biol. Chem. , vol.283 , pp. 9814-9819
    • Pasic, L.1    Kotova, T.2    Schafer, D.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.