메뉴 건너뛰기




Volumn 28, Issue 4, 2007, Pages 555-568

Analysis of the Function of Spire in Actin Assembly and Its Synergy with Formin and Profilin

Author keywords

CELLBIO

Indexed keywords

ACTIN; CELL PROTEIN; G ACTIN; LATRUNCULIN A; METHENAMINE; PROFILIN; SPIRE PROTEIN; THYMOSIN BETA4; UNCLASSIFIED DRUG;

EID: 36249032075     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molcel.2007.09.018     Document Type: Article
Times cited : (92)

References (39)
  • 1
    • 33644835262 scopus 로고    scopus 로고
    • The structural basis of actin interaction with multiple WH2/beta-thymosin motif-containing proteins
    • Aguda A.H., Xue B., Irobi E., Preat T., and Robinson R.C. The structural basis of actin interaction with multiple WH2/beta-thymosin motif-containing proteins. Structure 14 (2006) 469-476
    • (2006) Structure , vol.14 , pp. 469-476
    • Aguda, A.H.1    Xue, B.2    Irobi, E.3    Preat, T.4    Robinson, R.C.5
  • 2
    • 18044379419 scopus 로고    scopus 로고
    • Actin nucleation: spire-actin nucleator in a class of its own
    • Baum B., and Kunda P. Actin nucleation: spire-actin nucleator in a class of its own. Curr. Biol. 15 (2005) R305-R308
    • (2005) Curr. Biol. , vol.15
    • Baum, B.1    Kunda, P.2
  • 3
    • 0034664732 scopus 로고    scopus 로고
    • Ciboulot regulates actin assembly during Drosophila brain metamorphosis
    • Boquet I., Boujemaa R., Carlier M.F., and Preat T. Ciboulot regulates actin assembly during Drosophila brain metamorphosis. Cell 102 (2000) 797-808
    • (2000) Cell , vol.102 , pp. 797-808
    • Boquet, I.1    Boujemaa, R.2    Carlier, M.F.3    Preat, T.4
  • 4
    • 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., and 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 102 (2005) 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
  • 5
    • 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., and 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. 281 (2006) 26754-26767
    • (2006) J. Biol. Chem. , vol.281 , pp. 26754-26767
    • Chhabra, E.S.1    Higgs, H.N.2
  • 6
    • 33847420373 scopus 로고    scopus 로고
    • Mechanism of actin network attachment to moving membranes: barbed end capture by N-WASP WH2 domains
    • Co C., Wong D.T., Gierke S., Chang V., and Taunton J. Mechanism of actin network attachment to moving membranes: barbed end capture by N-WASP WH2 domains. Cell 128 (2007) 901-913
    • (2007) Cell , vol.128 , pp. 901-913
    • Co, C.1    Wong, D.T.2    Gierke, S.3    Chang, V.4    Taunton, J.5
  • 7
    • 0033965314 scopus 로고    scopus 로고
    • Control of actin assembly and disassembly at filament ends
    • Cooper J.A., and Schafer D.A. Control of actin assembly and disassembly at filament ends. Curr. Opin. Cell Biol. 12 (2000) 97-103
    • (2000) Curr. Opin. Cell Biol. , vol.12 , pp. 97-103
    • Cooper, J.A.1    Schafer, D.A.2
  • 8
    • 0033917806 scopus 로고    scopus 로고
    • Analysis of weight average sedimentation velocity data
    • Correia J.J. Analysis of weight average sedimentation velocity data. Methods Enzymol. 321 (2000) 81-100
    • (2000) Methods Enzymol. , vol.321 , pp. 81-100
    • Correia, J.J.1
  • 10
    • 0033588990 scopus 로고    scopus 로고
    • Activation of the CDC42 effector N-WASP by the Shigella flexneri IcsA protein promotes actin nucleation by Arp2/3 complex and bacterial actin-based motility
    • Egile C., Loisel T.P., Laurent V., Li R., Pantaloni D., Sansonetti P.J., and Carlier M.F. Activation of the CDC42 effector N-WASP by the Shigella flexneri IcsA protein promotes actin nucleation by Arp2/3 complex and bacterial actin-based motility. J. Cell Biol. 146 (1999) 1319-1332
    • (1999) J. Cell Biol. , vol.146 , pp. 1319-1332
    • Egile, C.1    Loisel, T.P.2    Laurent, V.3    Li, R.4    Pantaloni, D.5    Sansonetti, P.J.6    Carlier, M.F.7
  • 14
    • 21344433863 scopus 로고    scopus 로고
    • Fluorescence polarization/anisotropy approaches to study protein-ligand interactions: effects of errors and uncertainties
    • Jameson D.M., and Mocz G. Fluorescence polarization/anisotropy approaches to study protein-ligand interactions: effects of errors and uncertainties. Methods Mol. Biol. 305 (2005) 301-322
    • (2005) Methods Mol. Biol. , vol.305 , pp. 301-322
    • Jameson, D.M.1    Mocz, G.2
  • 15
    • 0030783012 scopus 로고    scopus 로고
    • Stathmin: a tubulin-sequestering protein which forms a ternary T2S complex with two tubulin molecules
    • Jourdain L., Curmi P., Sobel A., Pantloni D., and Carlier M.F. Stathmin: a tubulin-sequestering protein which forms a ternary T2S complex with two tubulin molecules. Biochemistry 36 (1997) 10817-10821
    • (1997) Biochemistry , vol.36 , pp. 10817-10821
    • Jourdain, L.1    Curmi, P.2    Sobel, A.3    Pantloni, D.4    Carlier, M.F.5
  • 16
    • 33747892855 scopus 로고    scopus 로고
    • Cellular functions of the Spir actin-nucleation factors
    • Kerkhoff E. Cellular functions of the Spir actin-nucleation factors. Trends Cell Biol. 16 (2006) 477-483
    • (2006) Trends Cell Biol. , vol.16 , pp. 477-483
    • Kerkhoff, E.1
  • 17
    • 33845395529 scopus 로고    scopus 로고
    • pEg6, a spire family member, is a maternal gene encoding a vegetally localized mRNA in Xenopus embryos
    • Le Goff C., Laurent V., Le Bon K., Tanguy G., Couturier A., Le Goff X., and Le Guellec R. pEg6, a spire family member, is a maternal gene encoding a vegetally localized mRNA in Xenopus embryos. Biol. Cell 98 (2006) 697-708
    • (2006) Biol. Cell , vol.98 , pp. 697-708
    • Le Goff, C.1    Laurent, V.2    Le Bon, K.3    Tanguy, G.4    Couturier, A.5    Le Goff, X.6    Le Guellec, R.7
  • 18
    • 33846817369 scopus 로고    scopus 로고
    • Structural basis for the actin-binding function of missing-in-metastasis
    • Lee S.H., Kerff F., Chereau D., Ferron F., Klug A., and Dominguez R. Structural basis for the actin-binding function of missing-in-metastasis. Structure 15 (2007) 145-155
    • (2007) Structure , vol.15 , pp. 145-155
    • Lee, S.H.1    Kerff, F.2    Chereau, D.3    Ferron, F.4    Klug, A.5    Dominguez, R.6
  • 19
    • 0033533789 scopus 로고    scopus 로고
    • Reconstitution of actin-based motility of Listeria and Shigella using pure proteins
    • Loisel T.P., Boujemaa R., Pantaloni D., and Carlier M.F. Reconstitution of actin-based motility of Listeria and Shigella using pure proteins. Nature 401 (1999) 613-616
    • (1999) Nature , vol.401 , pp. 613-616
    • Loisel, T.P.1    Boujemaa, R.2    Pantaloni, D.3    Carlier, M.F.4
  • 20
    • 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., and Schupbach T. cappuccino and spire: two unique maternal-effect loci required for both the anteroposterior and dorsoventral patterns of the Drosophila embryo. Genes Dev. 3 (1989) 1437-1452
    • (1989) Genes Dev. , vol.3 , pp. 1437-1452
    • Manseau, L.J.1    Schupbach, T.2
  • 21
    • 0030036816 scopus 로고    scopus 로고
    • Profilin is required for posterior patterning of the Drosophila oocyte
    • Manseau L., Calley J., and Phan H. Profilin is required for posterior patterning of the Drosophila oocyte. Development 122 (1996) 2109-2116
    • (1996) Development , vol.122 , pp. 2109-2116
    • Manseau, L.1    Calley, J.2    Phan, H.3
  • 22
    • 0027772556 scopus 로고
    • How profilin promotes filament assembly in the presence of thymosinβ4
    • Pantaloni D., and Carlier M.-F. How profilin promotes filament assembly in the presence of thymosinβ4. Cell 75 (1993) 1007-1014
    • (1993) Cell , vol.75 , pp. 1007-1014
    • Pantaloni, D.1    Carlier, M.-F.2
  • 23
    • 0033771755 scopus 로고    scopus 로고
    • The Arp2/3 complex branches filament barbed ends: functional antagonism with capping proteins
    • Pantaloni D., Boujemaa R., Didry D., Gounon P., and Carlier M.F. The Arp2/3 complex branches filament barbed ends: functional antagonism with capping proteins. Nat. Cell Biol. 2 (2000) 385-391
    • (2000) Nat. Cell Biol. , vol.2 , pp. 385-391
    • Pantaloni, D.1    Boujemaa, R.2    Didry, D.3    Gounon, P.4    Carlier, M.F.5
  • 24
    • 0037138384 scopus 로고    scopus 로고
    • WH2 domain: a small, versatile adapter for actin monomers
    • Paunola E., Mattila P.K., and Lappalainen P. WH2 domain: a small, versatile adapter for actin monomers. FEBS Lett. 513 (2002) 92-97
    • (2002) FEBS Lett. , vol.513 , pp. 92-97
    • Paunola, E.1    Mattila, P.K.2    Lappalainen, P.3
  • 25
    • 33745216899 scopus 로고    scopus 로고
    • Improved methods for fitting sedimentation coefficient distributions derived from time-derivative techniques
    • Philo J.S. Improved methods for fitting sedimentation coefficient distributions derived from time-derivative techniques. Anal. Biochem. 354 (2006) 238-246
    • (2006) Anal. Biochem. , vol.354 , pp. 238-246
    • Philo, J.S.1
  • 26
  • 27
    • 33748994545 scopus 로고    scopus 로고
    • Rho GTPases and actin dynamics in membrane protrusions and vesicle trafficking
    • Ridley A.J. Rho GTPases and actin dynamics in membrane protrusions and vesicle trafficking. Trends Cell Biol. 16 (2006) 522-529
    • (2006) Trends Cell Biol. , vol.16 , pp. 522-529
    • Ridley, A.J.1
  • 28
    • 7044224754 scopus 로고    scopus 로고
    • Formin is a processive motor that requires profilin to accelerate actin assembly and associated ATP hydrolysis
    • Romero S., Le Clainche C., Didry D., Egile C., Pantaloni D., and Carlier M.F. Formin is a processive motor that requires profilin to accelerate actin assembly and associated ATP hydrolysis. Cell 119 (2004) 419-429
    • (2004) Cell , vol.119 , pp. 419-429
    • Romero, S.1    Le Clainche, C.2    Didry, D.3    Egile, C.4    Pantaloni, D.5    Carlier, M.F.6
  • 29
    • 34247263230 scopus 로고    scopus 로고
    • How ATP hydrolysis controls filament assembly from profilin-actin: implication for formin processivity
    • Romero S., Didry D., Larquet E., Boisset N., Pantaloni D., and Carlier M.F. How ATP hydrolysis controls filament assembly from profilin-actin: implication for formin processivity. J. Biol. Chem. 282 (2007) 8435-8445
    • (2007) J. Biol. Chem. , vol.282 , pp. 8435-8445
    • Romero, S.1    Didry, D.2    Larquet, E.3    Boisset, N.4    Pantaloni, D.5    Carlier, M.F.6
  • 31
    • 0034009520 scopus 로고    scopus 로고
    • Size distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and lamm equation modeling
    • Schuck P. Size distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and lamm equation modeling. Biophys. Chem. 78 (2000) 1606-1619
    • (2000) Biophys. Chem. , vol.78 , pp. 1606-1619
    • Schuck, P.1
  • 32
    • 1642298085 scopus 로고    scopus 로고
    • A comparison of weight average and direct boundary fitting of sedimentation velocity data for indefinite polymerizing systems
    • Sontag C.A., Stafford W.F., and Correia J.J. A comparison of weight average and direct boundary fitting of sedimentation velocity data for indefinite polymerizing systems. Biophys. Chem. 108 (2004) 215-230
    • (2004) Biophys. Chem. , vol.108 , pp. 215-230
    • Sontag, C.A.1    Stafford, W.F.2    Correia, J.J.3
  • 33
    • 0026747656 scopus 로고
    • Boundary analysis in sedimentation transport experiments: a procedure for obtaining sedimentation coefficient distributions using the time derivative of the concentration profile
    • Stafford W.F. Boundary analysis in sedimentation transport experiments: a procedure for obtaining sedimentation coefficient distributions using the time derivative of the concentration profile. Anal. Biochem. 203 (1992) 295-301
    • (1992) Anal. Biochem. , vol.203 , pp. 295-301
    • Stafford, W.F.1
  • 34
    • 1642368109 scopus 로고    scopus 로고
    • Analysis of heterologous interacting systems by sedimentation velocity: curve fitting algorithms for estimation of sedimentation coefficients, equilibrium and kinetic constants
    • Stafford III W.F., and Sherwood P.J. Analysis of heterologous interacting systems by sedimentation velocity: curve fitting algorithms for estimation of sedimentation coefficients, equilibrium and kinetic constants. Biophys. Chem. 108 (2004) 231-243
    • (2004) Biophys. Chem. , vol.108 , pp. 231-243
    • Stafford III, W.F.1    Sherwood, P.J.2
  • 35
    • 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., and 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 1 (2007) 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
  • 37
    • 33646013893 scopus 로고    scopus 로고
    • Profilin: emerging concepts and lingering misconceptions
    • Yarmola E.G., and Bubb M.R. Profilin: emerging concepts and lingering misconceptions. Trends Biochem. Sci. 31 (2006) 197-205
    • (2006) Trends Biochem. Sci. , vol.31 , pp. 197-205
    • Yarmola, E.G.1    Bubb, M.R.2
  • 38
    • 0035824653 scopus 로고    scopus 로고
    • Formation and implications of a ternary complex of profilin, thymosin beta 4, and actin
    • Yarmola E.G., Parikh S., and Bubb M.R. Formation and implications of a ternary complex of profilin, thymosin beta 4, and actin. J. Biol. Chem. 276 (2001) 45555-45563
    • (2001) J. Biol. Chem. , vol.276 , pp. 45555-45563
    • Yarmola, E.G.1    Parikh, S.2    Bubb, M.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.