메뉴 건너뛰기




Volumn 287, Issue 41, 2012, Pages 34646-34649

Interactions of isolated C-terminal fragments of neural Wiskott-Aldrich syndrome protein (N-WASP) with actin and Arp2/3 complex

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN FILAMENT; ARP2/3 COMPLEX; ASYMMETRIC UNIT; BRANCHING PROCESS; C-TERMINAL DOMAINS; C-TERMINAL FRAGMENTS; CONSTITUTIVELY ACTIVES; PROFILIN; PROTEIN CRYSTALLOGRAPHY; SPECTROFLUORIMETRIC METHODS; TERNARY COMPLEX; WISKOTT-ALDRICH SYNDROME PROTEINS;

EID: 84867247557     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.394361     Document Type: Article
Times cited : (37)

References (71)
  • 1
    • 78049296901 scopus 로고    scopus 로고
    • WASH, WHAMM, and JMY. Regulation of Arp2/3 complex and beyond
    • Rottner, K., Hänisch, J., and Campellone, K. G. (2010) WASH, WHAMM, and JMY. Regulation of Arp2/3 complex and beyond. Trends Cell Biol. 20, 650-661
    • (2010) Trends Cell Biol. , vol.20 , pp. 650-661
    • Rottner, K.1    Hänisch, J.2    Campellone, K.G.3
  • 2
    • 77955605563 scopus 로고    scopus 로고
    • WASP family proteins. Their evolution and its physiological implications
    • Veltman, D. M., and Insall, R. H. (2010) WASP family proteins. Their evolution and its physiological implications. Mol. Biol. Cell 21, 2880-2893
    • (2010) Mol. Biol. Cell , vol.21 , pp. 2880-2893
    • Veltman, D.M.1    Insall, R.H.2
  • 3
    • 84858136256 scopus 로고    scopus 로고
    • Evolution of the eukaryotic ARP2/3 activators of the WASP family. WASP, WAVE, WASH, and WHAMM, and the proposed new family members WAWH and WAML
    • Kollmar, M., Lbik, D., and Enge, S. (2012) Evolution of the eukaryotic ARP2/3 activators of the WASP family. WASP, WAVE, WASH, and WHAMM, and the proposed new family members WAWH and WAML. BMC Res. Notes 5, 88
    • (2012) BMC Res. Notes , vol.5 , pp. 88
    • Kollmar, M.1    Lbik, D.2    Enge, S.3
  • 4
    • 0033620689 scopus 로고    scopus 로고
    • Arp2/3 complex and actin depolymerizing factor/cofilin in dendritic organization and treadmilling of actin filament array in lamellipodia
    • DOI 10.1083/jcb.145.5.1009
    • Svitkina, T. M., and Borisy, G. G. (1999) Arp2/3 complex and actin depolymerizing factor/cofilin in dendritic organization and treadmilling of actin filament array in lamellipodia. J. Cell Biol. 145, 1009-1026 (Pubitemid 29270059)
    • (1999) Journal of Cell Biology , vol.145 , Issue.5 , pp. 1009-1026
    • Svitkina, T.M.1    Borisy, G.G.2
  • 5
    • 33845729059 scopus 로고    scopus 로고
    • The WASP-WAVE protein network: Connecting the membrane to the cytoskeleton
    • DOI 10.1038/nrm2069, PII NRM2069
    • Takenawa, T., and Suetsugu, S. (2007) The WASP-WAVE protein network. Connecting the membrane to the cytoskeleton. Nat. Rev. Mol. Cell Biol. 8, 37-48 (Pubitemid 46012013)
    • (2007) Nature Reviews Molecular Cell Biology , vol.8 , Issue.1 , pp. 37-48
    • Takenawa, T.1    Suetsugu, S.2
  • 6
    • 36348952157 scopus 로고    scopus 로고
    • Wiskott-Aldrich syndrome protein is a key regulator of the phagocytic cup formation in macrophages
    • DOI 10.1074/jbc.M705999200
    • Tsuboi, S., and Meerloo, J. (2007) Wiskott-Aldrich syndrome protein is a key regulator of the phagocytic cup formation in macrophages. J. Biol. Chem. 282, 34194-34203 (Pubitemid 350159472)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.47 , pp. 34194-34203
    • Tsuboi, S.1    Meerloo, J.2
  • 7
    • 34047117842 scopus 로고    scopus 로고
    • T-cell-receptor-dependent actin regulatory mechanisms
    • DOI 10.1242/jcs.000786
    • Huang, Y., and Burkhardt, J. K. (2007) T-cell receptor-dependent actin regulatory mechanisms. J. Cell Sci. 120, 723-730 (Pubitemid 46523474)
    • (2007) Journal of Cell Science , vol.120 , Issue.5 , pp. 723-730
    • Huang, Y.1    Burkhardt, J.K.2
  • 8
    • 47049098701 scopus 로고    scopus 로고
    • N-WASP and the Arp2/3 complex are critical regulators of actin in the development of dendritic spines and synapses
    • Wegner, A. M., Nebhan, C. A., Hu, L., Majumdar, D., Meier, K. M., Weaver, A. M., and Webb, D. J. (2008) N-WASP and the Arp2/3 complex are critical regulators of actin in the development of dendritic spines and synapses. J. Biol. Chem. 283, 15912-15920
    • (2008) J. Biol. Chem. , vol.283 , pp. 15912-15920
    • Wegner, A.M.1    Nebhan, C.A.2    Hu, L.3    Majumdar, D.4    Meier, K.M.5    Weaver, A.M.6    Webb, D.J.7
  • 9
    • 46149096223 scopus 로고    scopus 로고
    • WHAMM Is an Arp2/3 Complex Activator That Binds Microtubules and Functions in ER to Golgi Transport
    • DOI 10.1016/j.cell.2008.05.032, PII S0092867408006934
    • Campellone, K. G., Webb, N. J., Znameroski, E. A., and Welch, M. D. (2008) WHAMM is an Arp2/3 complex activator that binds microtubules and functions in ER to Golgi transport. Cell 134, 148-161 (Pubitemid 351905739)
    • (2008) Cell , vol.134 , Issue.1 , pp. 148-161
    • Campellone, K.G.1    Webb, N.J.2    Znameroski, E.A.3    Welch, M.D.4
  • 10
    • 71549146571 scopus 로고    scopus 로고
    • The Arp2/3 activator WASH controls the fission of endosomes through a large multiprotein complex
    • Derivery, E., Sousa, C., Gautier, J. J., Lombard, B., Loew, D., and Gautreau, A. (2009) The Arp2/3 activator WASH controls the fission of endosomes through a large multiprotein complex. Dev. Cell. 17, 712-723
    • (2009) Dev. Cell. , vol.17 , pp. 712-723
    • Derivery, E.1    Sousa, C.2    Gautier, J.J.3    Lombard, B.4    Loew, D.5    Gautreau, A.6
  • 11
    • 77953757324 scopus 로고    scopus 로고
    • WASH and WAVE actin regulators of the Wiskott-Aldrich syndrome protein (WASP) family are controlled by analogous structurally related complexes
    • Jia, D., Gomez, T. S., Metlagel, Z., Umetani, J., Otwinowski, Z., Rosen, M. K., and Billadeau, D. D. (2010) WASH and WAVE actin regulators of the Wiskott-Aldrich syndrome protein (WASP) family are controlled by analogous structurally related complexes. Proc. Natl. Acad. Sci. U.S.A. 107, 10442-10447
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 10442-10447
    • Jia, D.1    Gomez, T.S.2    Metlagel, Z.3    Umetani, J.4    Otwinowski, Z.5    Rosen, M.K.6    Billadeau, D.D.7
  • 12
    • 84861926483 scopus 로고    scopus 로고
    • The Arp2/3 complex is required for lamellipodia extension and directional fibroblast cell migration
    • Suraneni, P., Rubinstein, B., Unruh, J. R., Durnin, M., Hanein, D., and Li, R. (2012) The Arp2/3 complex is required for lamellipodia extension and directional fibroblast cell migration. J. Cell Biol. 197, 239-251
    • (2012) J. Cell Biol. , vol.197 , pp. 239-251
    • Suraneni, P.1    Rubinstein, B.2    Unruh, J.R.3    Durnin, M.4    Hanein, D.5    Li, R.6
  • 13
    • 45849083156 scopus 로고    scopus 로고
    • Arp2/3 controls the motile behavior of N-WASP-functionalized GUVs and modulates N-WASP surface distribution by mediating transient links with actin filaments
    • Delatour, V., Helfer, E., Didry, D., Lê, K. H., Gaucher, J. F., Carlier, M. F., and Romet-Lemonne, G. (2008) Arp2/3 controls the motile behavior of N-WASP-functionalized GUVs and modulates N-WASP surface distribution by mediating transient links with actin filaments. Biophys. J. 94, 4890-4905
    • (2008) Biophys. J. , vol.94 , pp. 4890-4905
    • Delatour, V.1    Helfer, E.2    Didry, D.3    Lê, K.H.4    Gaucher, J.F.5    Carlier, M.F.6    Romet-Lemonne, G.7
  • 14
    • 61949147263 scopus 로고    scopus 로고
    • The rate of N-WASP exchange limits the extent of ARP2/3-complex-dependent actin-based motility
    • Weisswange, I., Newsome, T. P., Schleich, S., and Way, M. (2009) The rate of N-WASP exchange limits the extent of ARP2/3-complex-dependent actin-based motility. Nature 458, 87-91
    • (2009) Nature , vol.458 , pp. 87-91
    • Weisswange, I.1    Newsome, T.P.2    Schleich, S.3    Way, M.4
  • 15
    • 0033740788 scopus 로고    scopus 로고
    • Two tandem verprolin homology domains are necessary for a strong activation of Arp2/3 complex-induced actin polymerization and induction of microspike formation by N-WASP
    • Yamaguchi, H., Miki, H., Suetsugu, S., Ma, L., Kirschner, M. W., and Takenawa, T. (2000) Two tandem verprolin homology domains are necessary for a strong activation of Arp2/3 complex-induced actin polymerization and induction of microspike formation by N-WASP. Proc. Natl. Acad. Sci. U.S.A. 91, 12631-12636
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 12631-12636
    • Yamaguchi, H.1    Miki, H.2    Suetsugu, S.3    Ma, L.4    Kirschner, M.W.5    Takenawa, T.6
  • 16
    • 0035846598 scopus 로고    scopus 로고
    • Different WASP family proteins stimulate different Arp2/3 complex-dependent actin-nucleating activities
    • DOI 10.1016/S0960-9822(01)00603-0
    • Zalevsky, J., Lempert, L., Kranitz, H., and Mullins, R. D. (2001) Different WASP family proteins stimulate different Arp2/3 complex-dependent actin-nucleating activities. Curr. Biol. 11, 1903-1913 (Pubitemid 33146416)
    • (2001) Current Biology , vol.11 , Issue.24 , pp. 1903-1913
    • Zalevsky, J.1    Lempert, L.2    Kranitz, H.3    Mullins, R.D.4
  • 18
    • 0034911925 scopus 로고    scopus 로고
    • Regulation of actin filament network formation through Arp2/3 complex: Activation by a diverse array of proteins
    • DOI 10.1146/annurev.biochem.70.1.649
    • Higgs, H. N., and Pollard, T. D. (2001) Regulation of actin filament network formation through ARP2/3 complex. Activation by a diverse array of proteins. Annu. Rev. Biochem. 70, 649-676 (Pubitemid 32662221)
    • (2001) Annual Review of Biochemistry , vol.70 , pp. 649-676
    • Higgs, H.N.1    Pollard, T.D.2
  • 19
    • 21244446303 scopus 로고    scopus 로고
    • Acceleration of yeast actin polymerization by yeast Arp2/3 complex does not require and Arp2/3 complex activating protein
    • Wen, K. K., and Rubenstein, P. A. (2005) Acceleration of yeast actin polymerization by yeast Arp2/3 complex does not require and Arp2/3 complex activating protein. J. Biol. Chem. 280, 24168-24174
    • (2005) J. Biol. Chem. , vol.280 , pp. 24168-24174
    • Wen, K.K.1    Rubenstein, P.A.2
  • 20
    • 0037415575 scopus 로고    scopus 로고
    • A biomimetic motility assay provides insight into the mechanism of actin-based motility
    • DOI 10.1083/jcb.200207148
    • Wiesner, S., Helfer, E., Didry, D., Ducouret, G., Lafuma, F., Carlier, M. F., and Pantaloni, D. (2003) A biomimetic motility assay provides insight into the mechanism of actin-based motility. J. Cell Biol. 160, 387-398 (Pubitemid 36182729)
    • (2003) Journal of Cell Biology , vol.160 , Issue.3 , pp. 387-398
    • Wiesner, S.1    Helfer, E.2    Didry, D.3    Ducouret, G.4    Lafuma, F.5    Carlier, M.-F.6    Pantaloni, D.7
  • 21
    • 33847315536 scopus 로고    scopus 로고
    • Spatial and temporal relationships between actin filament nucleation, capping, and disassembly
    • Iwasa, J. H., and Mullins, R. D. (2007) Spatial and temporal relationships between actin filament nucleation, capping, and disassembly. Curr. Biol. 17, 395-406
    • (2007) Curr. Biol. , vol.17 , pp. 395-406
    • Iwasa, J.H.1    Mullins, R.D.2
  • 24
    • 43749107589 scopus 로고    scopus 로고
    • Pathway of actin filament branch formation by Arp2/3 complex
    • Beltzner, C. C., and Pollard, T. D. (2008) Pathway of actin filament branch formation by Arp2/3 complex. J. Biol. Chem. 283, 7135-7144
    • (2008) J. Biol. Chem. , vol.283 , pp. 7135-7144
    • Beltzner, C.C.1    Pollard, T.D.2
  • 25
    • 42949099523 scopus 로고    scopus 로고
    • X-Ray Scattering Study of Activated Arp2/3 Complex with Bound Actin-WCA
    • DOI 10.1016/j.str.2008.02.013, PII S0969212608001020
    • Boczkowska, M., Rebowski, G., Petoukhov, M. V., Hayes, D. B., Svergun, D. I., and Dominguez, R. (2008) X-ray scattering study of activated Arp2/3 complex with bound actin-WCA. Structure 16, 695-704 (Pubitemid 351626898)
    • (2008) Structure , vol.16 , Issue.5 , pp. 695-704
    • Boczkowska, M.1    Rebowski, G.2    Petoukhov, M.V.3    Hayes, D.B.4    Svergun, D.I.5    Dominguez, R.6
  • 27
    • 80051977000 scopus 로고    scopus 로고
    • Structural and biochemical characterization of two binding sites for nucleation-promoting factor WASp-VCA on Arp2/3 complex
    • Ti, S. C., Jurgenson, C. T., Nolen, B. J., and Pollard, T. D. (2011) Structural and biochemical characterization of two binding sites for nucleation-promoting factor WASp-VCA on Arp2/3 complex. Proc. Natl. Acad. Sci. U.S.A. 108, E463-E471
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108
    • Ti, S.C.1    Jurgenson, C.T.2    Nolen, B.J.3    Pollard, T.D.4
  • 29
    • 70450245305 scopus 로고    scopus 로고
    • Actin filament nucleation and elongation factors. Structure-function relationships
    • Dominguez, R. (2009) Actin filament nucleation and elongation factors. Structure-function relationships. Crit. Rev. Biochem. Mol. Biol. 44, 351-366
    • (2009) Crit. Rev. Biochem. Mol. Biol. , vol.44 , pp. 351-366
    • Dominguez, R.1
  • 30
    • 2542421811 scopus 로고    scopus 로고
    • The β-thymosin/WH2 domain: Structural basis for the switch from inhibition to promotion of actin assembly
    • DOI 10.1016/S0092-8674(04)00403-9, PII S0092867404004039
    • Hertzog, M., van Heijenoort, C., Didry, D., Gaudier, M., Coutant, J., Gigant, B., Didelot, G., Préat, T., Knossow, M., Guittet, E., and Carlier, M. F. (2004) The β-thymosin/WH2 domain; structural basis for the switch from inhibition to promotion of actin assembly. Cell 117, 611-623 (Pubitemid 38692527)
    • (2004) Cell , vol.117 , Issue.5 , pp. 611-623
    • Hertzog, M.1    Van Heijenoort, C.2    Didry, D.3    Gaudier, M.4    Coutant, J.5    Gigant, B.6    Didelot, G.7    Preat, T.8    Knossow, M.9    Guittet, E.10    Carlier, M.-F.11
  • 31
    • 52949096103 scopus 로고    scopus 로고
    • Spire and Cordon-bleu. Multifunctional regulators of actin dynamics
    • Renault, L., Bugyi, B., and Carlier, M. F. (2008) Spire and Cordon-bleu. Multifunctional regulators of actin dynamics. Trends Cell Biol. 18, 494-504
    • (2008) Trends Cell Biol. , vol.18 , pp. 494-504
    • Renault, L.1    Bugyi, B.2    Carlier, M.F.3
  • 32
    • 80052083395 scopus 로고    scopus 로고
    • Control of actin assembly by the WH2 domains and their multifunctional tandem repeats in Spire and Cordon-Bleu
    • Carlier, M. F., Husson, C., Renault, L., and Didry, D. (2011) Control of actin assembly by the WH2 domains and their multifunctional tandem repeats in Spire and Cordon-Bleu. Int. Rev. Cell Mol. Biol. 290, 55-85
    • (2011) Int. Rev. Cell Mol. Biol. , vol.290 , pp. 55-85
    • Carlier, M.F.1    Husson, C.2    Renault, L.3    Didry, D.4
  • 33
    • 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
    • DOI 10.1074/jbc.M507470200
    • Kelly, A. E., Kranitz, H., Dötsch, V., and Mullins, R. D. (2006) 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. 281, 10589-10597 (Pubitemid 43864601)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.15 , pp. 10589-10597
    • Kelly, A.E.1    Kranitz, H.2    Dotsch, V.3    Mullins, R.D.4
  • 34
    • 0028908914 scopus 로고
    • Quantitation of Cap Z in conventional actin preparations and methods for further purification of actin
    • Casella, J. F., Barron-Casella, E. A., and Torres, M. A. (1995) Quantitation of Cap Z in conventional actin preparations and methods for further purification of actin. Cell Motil. Cytoskeleton 30, 164-170
    • (1995) Cell Motil. Cytoskeleton , vol.30 , pp. 164-170
    • Casella, J.F.1    Barron-Casella, E.A.2    Torres, M.A.3
  • 35
    • 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
    • DOI 10.1083/jcb.146.6.1319
    • Egile, C., Loisel, T. P., Laurent, V., Li, R., Pantaloni, D., Sansonetti, P. J., and Carlier, M. F. (1999) 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, 1319-1332 (Pubitemid 29477698)
    • (1999) Journal of Cell Biology , vol.146 , Issue.6 , 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
  • 36
    • 0029018327 scopus 로고
    • Tight regulation, modulation, and high level expression by vectors containing the arabinose PBAD promoter
    • Guzman, L. M., Belin, D., Carson, M. J., and Beckwith, J. (1995) Tight regulation, modulation, and high level expression by vectors containing the arabinose PBAD promoter. J. Bacteriol. 177, 4121-4130
    • (1995) J. Bacteriol. , vol.177 , pp. 4121-4130
    • Guzman, L.M.1    Belin, D.2    Carson, M.J.3    Beckwith, J.4
  • 37
    • 0028871804 scopus 로고
    • How to measure and predict the molar absorption coefficient of a protein
    • Pace, C. N., Vajdos, F., Fee, L., Grimsley, G., and Gray, T. (1995) How to measure and predict the molar absorption coefficient of a protein. Protein Sci. 4, 2411-2423
    • (1995) Protein Sci. , vol.4 , pp. 2411-2423
    • Pace, C.N.1    Vajdos, F.2    Fee, L.3    Grimsley, G.4    Gray, T.5
  • 38
    • 71649092785 scopus 로고    scopus 로고
    • Read, R. J., and Sussman, J. L., eds Springer NATO Science Series, New York
    • Leslie, A. G., and Powell, H. R. (2007) in Evolving Methods for Macromolecular Crystallography (Read, R. J., and Sussman, J. L., eds) Vol. 245, pp. 41-45, Springer NATO Science Series, New York
    • (2007) Evolving Methods for Macromolecular Crystallography , vol.245 , pp. 41-45
    • Leslie, A.G.1    Powell, H.R.2
  • 40
    • 0037779022 scopus 로고    scopus 로고
    • A statistic for local intensity differences: Robustness to anisotropy and pseudo-centering and utility for detecting twinning
    • DOI 10.1107/S0907444903007947
    • Padilla, J. E., and Yeates, T. O. (2003) A statistic for local intensity differences. Robustness to anisotropy and pseudo-centering and utility for detecting twinning. Acta Crystallogr. D Biol. Crystallogr. 59, 1124-1130 (Pubitemid 36872347)
    • (2003) Acta Crystallographica Section D: Biological Crystallography , vol.59 , Issue.7 , pp. 1124-1130
    • Padilla, J.E.1    Yeates, T.O.2
  • 41
    • 84920325457 scopus 로고
    • AMoRe. An automated package for molecular replacement
    • Navaza, J. (1994) AMoRe. An automated package for molecular replacement. Acta Crystallogr. A 50, 157-163
    • (1994) Acta Crystallogr. A , vol.50 , pp. 157-163
    • Navaza, J.1
  • 46
    • 36249032075 scopus 로고    scopus 로고
    • Analysis of the Function of Spire in Actin Assembly and Its Synergy with Formin and Profilin
    • DOI 10.1016/j.molcel.2007.09.018, PII S1097276507006302
    • Bosch, M., Le, K. H., Bugyi, B., Correia, J. J., Renault, L., and Carlier, M. F. (2007) Analysis of the function of Spire in actin assembly and its synergy with formin and profilin. Mol. Cell 28, 555-568 (Pubitemid 350137795)
    • (2007) Molecular Cell , vol.28 , Issue.4 , pp. 555-568
    • Bosch, M.1    Le, K.H.D.2    Bugyi, B.3    Correia, J.J.4    Renault, L.5    Carlier, M.-F.6
  • 47
    • 79960930017 scopus 로고    scopus 로고
    • Cordon-Bleu uses WH2 domains as multifunctional dynamizers of actin filament assembly
    • Husson, C., Renault, L., Didry, D., Pantaloni, D., and Carlier, M. F. (2011) Cordon-Bleu uses WH2 domains as multifunctional dynamizers of actin filament assembly. Mol. Cell 43, 464-477
    • (2011) Mol. Cell , vol.43 , pp. 464-477
    • Husson, C.1    Renault, L.2    Didry, D.3    Pantaloni, D.4    Carlier, M.F.5
  • 48
    • 34548232365 scopus 로고    scopus 로고
    • Inference of Macromolecular Assemblies from Crystalline State
    • DOI 10.1016/j.jmb.2007.05.022, PII S0022283607006420
    • Krissinel, E., and Henrick, K. (2007) Inference of macromolecular assemblies from crystalline state. J. Mol. Biol. 372, 774-797 (Pubitemid 47321791)
    • (2007) Journal of Molecular Biology , vol.372 , Issue.3 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 49
    • 0025123333 scopus 로고
    • The structure of protein-protein recognition sites
    • Janin, J., and Chothia, C. (1990) The structure of protein-protein recognition sites. J. Biol. Chem. 265, 16027-16030
    • (1990) J. Biol. Chem. , vol.265 , pp. 16027-16030
    • Janin, J.1    Chothia, C.2
  • 50
    • 33846817369 scopus 로고    scopus 로고
    • Structural Basis for the Actin-Binding Function of Missing-in-Metastasis
    • DOI 10.1016/j.str.2006.12.005, PII S0969212607000275
    • Lee, S. H., Kerff, F., Chereau, D., Ferron, F., Klug, A., and Dominguez, R. (2007) Structural basis for the actin-binding function of missing-in-metastasis. Structure 15, 145-155 (Pubitemid 46209813)
    • (2007) Structure , vol.15 , Issue.2 , pp. 145-155
    • Lee, S.H.1    Kerff, F.2    Chereau, D.3    Ferron, F.4    Klug, A.5    Dominguez, R.6
  • 51
    • 0035958757 scopus 로고    scopus 로고
    • The crystal structure of uncomplexed actin in the ADR state
    • Otterbein, L. R., Graceffa, P., and Dominguez, R. (2001) The crystal structure of uncomplexed actin in the ADP state. Science 293, 708-711 (Pubitemid 32728675)
    • (2001) Science , vol.293 , Issue.5530 , pp. 708-711
    • Otterbein, L.R.1    Graceffa, P.2    Dominguez, R.3
  • 52
    • 33846020951 scopus 로고    scopus 로고
    • Crystal structures of expressed non-polymerizable monomeric actin in the ADP and ATP states
    • DOI 10.1074/jbc.M601973200
    • Rould, M. A., Wan, Q., Joel, P. B., Lowey, S., and Trybus, K. M. (2006) Crystal structures of expressed nonpolymerizable monomeric actin in the ADP and ATP states. J. Biol. Chem. 281, 31909-31919 (Pubitemid 46041453)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.42 , pp. 31909-31919
    • Rould, M.A.1    Wan, Q.2    Joel, P.B.3    Lowey, S.4    Trybus, K.M.5
  • 53
    • 0032006209 scopus 로고    scopus 로고
    • Systematic analysis of domain motions in proteins from conformational change: New results on citrate synthase and T4 lysozyme
    • DOI 10.1002/(SICI)1097-0134(19980201)30:2<144::AID-PROT4>3.0.CO;2-N
    • Hayward, S., and Berendsen, H. J. (1998) Systematic analysis of domain motions in proteins from conformational change. New results on citrate synthase and T4 lysozyme. Proteins 30, 144-154 (Pubitemid 28080149)
    • (1998) Proteins: Structure, Function and Genetics , vol.30 , Issue.2 , pp. 144-154
    • Hayward, S.1    Berendsen, H.J.C.2
  • 54
    • 0037188362 scopus 로고    scopus 로고
    • Actin filament barbed end elongation with nonmuscle MgATP-actin and MgADP-actin in the presence of profilin
    • DOI 10.1021/bi016083t
    • Kinosian, H. J., Selden, L. A., Gershman, L. C., and Estes, J. E. (2002) Actin filament barbed end elongation with nonmuscle MgATP-actin and MgADP-actin in the presence of profilin. Biochemistry 41, 6734-6743 (Pubitemid 34547364)
    • (2002) Biochemistry , vol.41 , Issue.21 , pp. 6734-6743
    • Kinosian, H.J.1    Selden, L.A.2    Gershman, L.C.3    Estes, J.E.4
  • 55
    • 0041589208 scopus 로고    scopus 로고
    • Depolymerization of actin filaments by profilin: Effects of profilin on capping protein function
    • DOI 10.1074/jbc.M302796200
    • Bubb, M. R., Yarmola, E. G., Gibson, B. G., and Southwick, F. S. (2003) Depolymerization of actin filaments by profilin. Effects of profilin on capping protein function. J. Biol. Chem. 278, 24629-24635 (Pubitemid 37548617)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.27 , pp. 24629-24635
    • Bubb, M.R.1    Yarmola, E.G.2    Gibson, B.G.3    Southwick, F.S.4
  • 57
    • 1042275583 scopus 로고    scopus 로고
    • A Dissection of Specific and Non-specific Protein-Protein Interfaces
    • DOI 10.1016/j.jmb.2003.12.073
    • Bahadur, R. P., Chakrabarti, P., Rodier, F., and Janin, J. (2004) A dissection of specific and nonspecific protein-protein interfaces. J. Mol. Biol. 336, 943-955 (Pubitemid 38201541)
    • (2004) Journal of Molecular Biology , vol.336 , Issue.4 , pp. 943-955
    • Bahadur, R.P.1    Chakrabarti, P.2    Rodier, F.3    Janin, J.4
  • 60
    • 13444292982 scopus 로고    scopus 로고
    • Drosophila Spire is an actin nucleation factor
    • DOI 10.1038/nature03241
    • Quinlan, M. E., Heuser, J. E., Kerkhoff, E., and Mullins, R. D. (2005) Drosophila Spire is an actin nucleation factor. Nature 433, 382-388 (Pubitemid 40203312)
    • (2005) Nature , vol.433 , Issue.7024 , pp. 382-388
    • Quinlan, M.E.1    Heuser, J.E.2    Kerkhoff, E.3    Mullins, R.D.4
  • 62
    • 66349133039 scopus 로고    scopus 로고
    • New players in actin polymerization. WH2-domain-containing actin nucleators
    • Qualmann, B., and Kessels, M. M. (2009) New players in actin polymerization. WH2-domain-containing actin nucleators. Trends Cell Biol. 19, 276-285
    • (2009) Trends Cell Biol. , vol.19 , pp. 276-285
    • Qualmann, B.1    Kessels, M.M.2
  • 63
    • 80052510630 scopus 로고    scopus 로고
    • A new twist in actin filament nucleation
    • Carlier, M. F. (2011) A new twist in actin filament nucleation. Nat. Struct. Mol. Biol. 18, 967-969
    • (2011) Nat. Struct. Mol. Biol. , vol.18 , pp. 967-969
    • Carlier, M.F.1
  • 65
    • 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. (2000) The Arp2/3 complex branches filament barbed ends. Functional antagonism with capping proteins. Nat. Cell Biol. 2, 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
  • 66
    • 33847420373 scopus 로고    scopus 로고
    • Mechanism of Actin Network Attachment to Moving Membranes: Barbed End Capture by N-WASP WH2 Domains
    • DOI 10.1016/j.cell.2006.12.049, PII S0092867407001316
    • Co, C., Wong, D. T., Gierke, S., Chang, V., and Taunton, J. (2007) Mechanism of actin network attachment to moving membranes. Barbed end capture by N-WASP WH2 domains. Cell 128, 901-913 (Pubitemid 46341410)
    • (2007) Cell , vol.128 , Issue.5 , pp. 901-913
    • Co, C.1    Wong, D.T.2    Gierke, S.3    Chang, V.4    Taunton, J.5
  • 68
    • 78049521359 scopus 로고    scopus 로고
    • VASP is a processive actin polymerase that requires monomeric actin for barbed end association
    • Hansen, S. D., and Mullins, R. D. (2010) VASP is a processive actin polymerase that requires monomeric actin for barbed end association. J. Cell Biol. 191, 571-584
    • (2010) J. Cell Biol. , vol.191 , pp. 571-584
    • Hansen, S.D.1    Mullins, R.D.2
  • 71
    • 84856295948 scopus 로고    scopus 로고
    • Individual actin filaments in a microfluidic flow reveal the mechanism of ATP hydrolysis and give insight into the properties of profilin
    • Jégou, A., Niedermayer, T., Orbán, J., Didry, D., Lipowsky, R., Carlier, M. F., and Romet-Lemonne, G. (2011) Individual actin filaments in a microfluidic flow reveal the mechanism of ATP hydrolysis and give insight into the properties of profilin. PloS Biol. e1001161
    • (2011) PloS Biol.
    • Jégou, A.1    Niedermayer, T.2    Orbán, J.3    Didry, D.4    Lipowsky, R.5    Carlier, M.F.6    Romet-Lemonne, G.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.