메뉴 건너뛰기




Volumn 540, Issue , 2014, Pages 95-117

Single-molecule studies of actin assembly and disassembly factors

Author keywords

Arp2 3 complex; Binding kinetics; Cofilin; Filament nucleation; Formin; Polymerization; Severing; Total internal reflection fluorescence

Indexed keywords

ACTIN; ACTIN RELATED PROTEIN 2-3 COMPLEX; APC PROTEIN; COFILIN; PROTEIN TAG;

EID: 84896375456     PISSN: 00766879     EISSN: 15577988     Source Type: Book Series    
DOI: 10.1016/B978-0-12-397924-7.00006-6     Document Type: Chapter
Times cited : (17)

References (44)
  • 1
    • 0035910096 scopus 로고    scopus 로고
    • Direct real-time observation of actin filament branching mediated by Arp2/3 complex using total internal reflection fluorescence microscopy
    • 10.1073/pnas.211556398
    • K.J. Amann, and T.D. Pollard Direct real-time observation of actin filament branching mediated by Arp2/3 complex using total internal reflection fluorescence microscopy Proceedings of the National Academy of Sciences of the United States of America 98 26 2001 15009 15013 10.1073/pnas.211556398
    • (2001) Proceedings of the National Academy of Sciences of the United States of America , vol.98 , Issue.26 , pp. 15009-15013
    • Amann, K.J.1    Pollard, T.D.2
  • 2
    • 0037284103 scopus 로고    scopus 로고
    • Total internal reflection fluorescence microscopy in cell biology
    • D. Axelrod Total internal reflection fluorescence microscopy in cell biology Methods in Enzymology 361 2003 1 33
    • (2003) Methods in Enzymology , vol.361 , pp. 1-33
    • Axelrod, D.1
  • 3
    • 43749107589 scopus 로고    scopus 로고
    • Pathway of actin filament branch formation by Arp2/3 complex
    • 10.1074/jbc.M705894200
    • C.C. Beltzner, and T.D. Pollard Pathway of actin filament branch formation by Arp2/3 complex The Journal of Biological Chemistry 283 11 2008 7135 7144 10.1074/jbc.M705894200
    • (2008) The Journal of Biological Chemistry , vol.283 , Issue.11 , pp. 7135-7144
    • Beltzner, C.C.1    Pollard, T.D.2
  • 4
    • 0034687235 scopus 로고    scopus 로고
    • Interactions of ADF/cofilin, Arp2/3 complex, capping protein and profilin in remodeling of branched actin filament networks
    • L. Blanchoin, T.D. Pollard, and R.D. Mullins Interactions of ADF/cofilin, Arp2/3 complex, capping protein and profilin in remodeling of branched actin filament networks Current Biology 10 20 2000 1273 1282
    • (2000) Current Biology , vol.10 , Issue.20 , pp. 1273-1282
    • Blanchoin, L.1    Pollard, T.D.2    Mullins, R.D.3
  • 5
    • 80053356578 scopus 로고    scopus 로고
    • Clathrin light chain directs endocytosis by influencing the binding of the yeast Hip1R homologue, Sla2, to F-actin
    • 10.1091/mbc.E11-07-0628
    • D.R. Boettner, H. Friesen, B. Andrews, and S.K. Lemmon Clathrin light chain directs endocytosis by influencing the binding of the yeast Hip1R homologue, Sla2, to F-actin Molecular Biology of the Cell 22 19 2011 3699 3714 10.1091/mbc.E11-07-0628
    • (2011) Molecular Biology of the Cell , vol.22 , Issue.19 , pp. 3699-3714
    • Boettner, D.R.1    Friesen, H.2    Andrews, B.3    Lemmon, S.K.4
  • 6
    • 84861708449 scopus 로고    scopus 로고
    • Rocket launcher mechanism of collaborative actin assembly defined by single-molecule imaging
    • 10.1126/science.1218062
    • D. Breitsprecher, R. Jaiswal, J.P. Bombardier, C.J. Gould, J. Gelles, and B.L. Goode Rocket launcher mechanism of collaborative actin assembly defined by single-molecule imaging Science 336 6085 2012 1164 1168 10.1126/science.1218062
    • (2012) Science , vol.336 , Issue.6085 , pp. 1164-1168
    • Breitsprecher, D.1    Jaiswal, R.2    Bombardier, J.P.3    Gould, C.J.4    Gelles, J.5    Goode, B.L.6
  • 7
    • 52649120304 scopus 로고    scopus 로고
    • Coronin 1B antagonizes cortactin and remodels Arp2/3-containing actin branches in lamellipodia
    • 10.1016/j.cell.2008.06.054
    • L. Cai, A.M. Makhov, D.A. Schafer, and J.E. Bear Coronin 1B antagonizes cortactin and remodels Arp2/3-containing actin branches in lamellipodia Cell 134 5 2008 828 842 10.1016/j.cell.2008.06.054
    • (2008) Cell , vol.134 , Issue.5 , pp. 828-842
    • Cai, L.1    Makhov, A.M.2    Schafer, D.A.3    Bear, J.E.4
  • 8
    • 64049091643 scopus 로고    scopus 로고
    • Cofilin dissociates Arp2/3 complex and branches from actin filaments
    • 10.1016/j.cub.2009.02.060
    • C. Chan, C.C. Beltzner, and T.D. Pollard Cofilin dissociates Arp2/3 complex and branches from actin filaments Current Biology 19 7 2009 537 545 10.1016/j.cub.2009.02.060
    • (2009) Current Biology , vol.19 , Issue.7 , pp. 537-545
    • Chan, C.1    Beltzner, C.C.2    Pollard, T.D.3
  • 9
    • 84871882289 scopus 로고    scopus 로고
    • Srv2/cyclase-associated protein forms hexameric shurikens that directly catalyze actin filament severing by cofilin
    • 10.1091/mbc.E12-08-0589
    • F. Chaudhry, D. Breitsprecher, K. Little, G. Sharov, O. Sokolova, and B.L. Goode Srv2/cyclase-associated protein forms hexameric shurikens that directly catalyze actin filament severing by cofilin Molecular Biology of the Cell 24 1 2013 31 41 10.1091/mbc.E12-08-0589
    • (2013) Molecular Biology of the Cell , vol.24 , Issue.1 , pp. 31-41
    • Chaudhry, F.1    Breitsprecher, D.2    Little, K.3    Sharov, G.4    Sokolova, O.5    Goode, B.L.6
  • 10
    • 0001908198 scopus 로고
    • Fitting and statistical analysis of single-channel records
    • Plenum New York
    • D. Colquhoun, and F.J. Sigworth Fitting and statistical analysis of single-channel records Single-channel recording 1983 Plenum New York 191 263
    • (1983) Single-channel Recording , pp. 191-263
    • Colquhoun, D.1    Sigworth, F.J.2
  • 11
    • 38049077956 scopus 로고    scopus 로고
    • Visualizing the splicing of single pre-mRNA molecules in whole cell extract
    • 10.1261/rna.794808
    • D.J. Crawford, A.A. Hoskins, L.J. Friedman, J. Gelles, and M.J. Moore Visualizing the splicing of single pre-mRNA molecules in whole cell extract RNA 14 1 2008 170 179 10.1261/rna.794808
    • (2008) RNA , vol.14 , Issue.1 , pp. 170-179
    • Crawford, D.J.1    Hoskins, A.A.2    Friedman, L.J.3    Gelles, J.4    Moore, M.J.5
  • 12
    • 0029977418 scopus 로고    scopus 로고
    • Methods of digital video microscopy for colloidal studies
    • 10.1006/jcis.1996.0217
    • J.C. Crocker, and D.G. Grier Methods of digital video microscopy for colloidal studies Journal of Colloid and Interface Science 179 1 1996 298 310 10.1006/jcis.1996.0217
    • (1996) Journal of Colloid and Interface Science , vol.179 , Issue.1 , pp. 298-310
    • Crocker, J.C.1    Grier, D.G.2
  • 13
    • 79951556468 scopus 로고    scopus 로고
    • New mechanisms and functions of actin nucleation
    • 10.1016/j.ceb.2010.10.007
    • E.N. Firat-Karalar, and M.D. Welch New mechanisms and functions of actin nucleation Current Opinion in Cell Biology 23 1 2011 4 13 10.1016/j.ceb.2010.10. 007
    • (2011) Current Opinion in Cell Biology , vol.23 , Issue.1 , pp. 4-13
    • Firat-Karalar, E.N.1    Welch, M.D.2
  • 14
    • 33746743013 scopus 로고    scopus 로고
    • Viewing dynamic assembly of molecular complexes by multi-wavelength single-molecule fluorescence
    • 10.1529/biophysj.106.084004
    • L.J. Friedman, J. Chung, and J. Gelles Viewing dynamic assembly of molecular complexes by multi-wavelength single-molecule fluorescence Biophysical Journal 91 3 2006 1023 1031 10.1529/biophysj.106.084004
    • (2006) Biophysical Journal , vol.91 , Issue.3 , pp. 1023-1031
    • Friedman, L.J.1    Chung, J.2    Gelles, J.3
  • 16
    • 77449152025 scopus 로고    scopus 로고
    • Direct observation of the uncapping of capping protein-capped actin filaments by CARMIL homology domain 3
    • 10.1074/jbc.M109.031203
    • I. Fujiwara, K. Remmert, and J.A. Hammer 3rd Direct observation of the uncapping of capping protein-capped actin filaments by CARMIL homology domain 3 The Journal of Biological Chemistry 285 4 2010 2707 2720 10.1074/jbc.M109.031203
    • (2010) The Journal of Biological Chemistry , vol.285 , Issue.4 , pp. 2707-2720
    • Fujiwara, I.1    Remmert, K.2    Hammer III, J.A.3
  • 17
    • 77953170746 scopus 로고    scopus 로고
    • GMF is a cofilin homolog that binds Arp2/3 complex to stimulate filament debranching and inhibit actin nucleation
    • 10.1016/j.cub.2010.03.026
    • M. Gandhi, B.A. Smith, M. Bovellan, V. Paavilainen, K. Daugherty-Clarke, and J. Gelles et al. GMF is a cofilin homolog that binds Arp2/3 complex to stimulate filament debranching and inhibit actin nucleation Current Biology 20 9 2010 861 867 10.1016/j.cub.2010.03.026
    • (2010) Current Biology , vol.20 , Issue.9 , pp. 861-867
    • Gandhi, M.1    Smith, B.A.2    Bovellan, M.3    Paavilainen, V.4    Daugherty-Clarke, K.5    Gelles, J.6
  • 18
    • 84859899534 scopus 로고    scopus 로고
    • Photophysics of fluorescent probes for single-molecule biophysics and super-resolution imaging
    • 10.1146/annurev-physchem-032210-103340
    • T. Ha, and P. Tinnefeld Photophysics of fluorescent probes for single-molecule biophysics and super-resolution imaging Annual Review of Physical Chemistry 63 2012 595 617 10.1146/annurev-physchem-032210-103340
    • (2012) Annual Review of Physical Chemistry , vol.63 , pp. 595-617
    • Ha, T.1    Tinnefeld, P.2
  • 19
    • 80053951342 scopus 로고    scopus 로고
    • Pathogens and polymers: Microbe-host interactions illuminate the cytoskeleton
    • 10.1083/jcb.201103148
    • C.M. Haglund, and M.D. Welch Pathogens and polymers: Microbe-host interactions illuminate the cytoskeleton The Journal of Cell Biology 195 1 2011 7 17 10.1083/jcb.201103148
    • (2011) The Journal of Cell Biology , vol.195 , Issue.1 , pp. 7-17
    • Haglund, C.M.1    Welch, M.D.2
  • 20
    • 78049521359 scopus 로고    scopus 로고
    • VASP is a processive actin polymerase that requires monomeric actin for barbed end association
    • 10.1083/jcb.201003014
    • S.D. Hansen, and R.D. Mullins VASP is a processive actin polymerase that requires monomeric actin for barbed end association The Journal of Cell Biology 191 3 2010 571 584 10.1083/jcb.201003014
    • (2010) The Journal of Cell Biology , vol.191 , Issue.3 , pp. 571-584
    • Hansen, S.D.1    Mullins, R.D.2
  • 21
    • 0029046139 scopus 로고
    • Flexibility of actin filaments derived from thermal fluctuations. Effect of bound nucleotide, phalloidin, and muscle regulatory proteins
    • H. Isambert, P. Venier, A.C. Maggs, A. Fattoum, R. Kassab, and D. Pantaloni et al. Flexibility of actin filaments derived from thermal fluctuations. Effect of bound nucleotide, phalloidin, and muscle regulatory proteins The Journal of Biological Chemistry 270 19 1995 11437 11444
    • (1995) The Journal of Biological Chemistry , vol.270 , Issue.19 , pp. 11437-11444
    • Isambert, H.1    Venier, P.2    Maggs, A.C.3    Fattoum, A.4    Kassab, R.5    Pantaloni, D.6
  • 22
    • 84882738424 scopus 로고    scopus 로고
    • A fluorogenic TMP-tag for high signal-to-background intracellular live cell imaging
    • 10.1021/cb300657r
    • C. Jing, and V.W. Cornish A fluorogenic TMP-tag for high signal-to-background intracellular live cell imaging ACS Chemical Biology 8 2013 1704 1712 10.1021/cb300657r
    • (2013) ACS Chemical Biology , vol.8 , pp. 1704-1712
    • Jing, C.1    Cornish, V.W.2
  • 23
    • 31044433924 scopus 로고    scopus 로고
    • Control of the assembly of ATP- and ADP-actin by formins and profilin
    • 10.1016/j.cell.2005.11.038
    • D.R. Kovar, E.S. Harris, R. Mahaffy, H.N. Higgs, and T.D. Pollard Control of the assembly of ATP- and ADP-actin by formins and profilin Cell 124 2 2006 423 435 10.1016/j.cell.2005.11.038
    • (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
  • 24
    • 18844389128 scopus 로고    scopus 로고
    • Real-time measurements of actin filament polymerization by total internal reflection fluorescence microscopy
    • 10.1529/biophysj.104.047399
    • J.R. Kuhn, and T.D. Pollard Real-time measurements of actin filament polymerization by total internal reflection fluorescence microscopy Biophysical Journal 88 2 2005 1387 1402 10.1529/biophysj.104.047399
    • (2005) Biophysical Journal , vol.88 , Issue.2 , pp. 1387-1402
    • Kuhn, J.R.1    Pollard, T.D.2
  • 25
    • 33748926752 scopus 로고    scopus 로고
    • Stoichiometry and turnover in single, functioning membrane protein complexes
    • 10.1038/nature05135
    • M.C. Leake, J.H. Chandler, G.H. Wadhams, F. Bai, R.M. Berry, and J.P. Armitage Stoichiometry and turnover in single, functioning membrane protein complexes Nature 443 7109 2006 355 358 10.1038/nature05135
    • (2006) Nature , vol.443 , Issue.7109 , pp. 355-358
    • Leake, M.C.1    Chandler, J.H.2    Wadhams, G.H.3    Bai, F.4    Berry, R.M.5    Armitage, J.P.6
  • 26
    • 79951670919 scopus 로고    scopus 로고
    • Cyanine dyes in biophysical research: The photophysics of polymethine fluorescent dyes in biomolecular environments
    • 10.1017/S0033583510000247
    • M. Levitus, and S. Ranjit Cyanine dyes in biophysical research: The photophysics of polymethine fluorescent dyes in biomolecular environments Quarterly Reviews of Biophysics 44 1 2011 123 151 10.1017/S0033583510000247
    • (2011) Quarterly Reviews of Biophysics , vol.44 , Issue.1 , pp. 123-151
    • Levitus, M.1    Ranjit, S.2
  • 27
    • 33746646463 scopus 로고    scopus 로고
    • Arp2/3 ATP hydrolysis-catalysed branch dissociation is critical for endocytic force generation
    • 10.1038/ncb1443
    • A.C. Martin, M.D. Welch, and D.G. Drubin Arp2/3 ATP hydrolysis-catalysed branch dissociation is critical for endocytic force generation Nature Cell Biology 8 8 2006 826 833 10.1038/ncb1443
    • (2006) Nature Cell Biology , vol.8 , Issue.8 , pp. 826-833
    • Martin, A.C.1    Welch, M.D.2    Drubin, D.G.3
  • 29
    • 78650988290 scopus 로고    scopus 로고
    • Rotational movement of the formin mDia1 along the double helical strand of an actin filament
    • 10.1126/science.1197692
    • H. Mizuno, C. Higashida, Y. Yuan, T. Ishizaki, S. Narumiya, and N. Watanabe Rotational movement of the formin mDia1 along the double helical strand of an actin filament Science (New York, N.Y.) 331 6013 2011 80 83 10.1126/science.1197692
    • (2011) Science (New York, N.Y.) , vol.331 , Issue.6013 , pp. 80-83
    • Mizuno, H.1    Higashida, C.2    Yuan, Y.3    Ishizaki, T.4    Narumiya, S.5    Watanabe, N.6
  • 30
    • 33747830489 scopus 로고    scopus 로고
    • Quantitative modeling in cell biology: What is it good for?
    • 10.1016/j.devcel.2006.08.004
    • A. Mogilner, R. Wollman, and W.F. Marshall Quantitative modeling in cell biology: What is it good for? Developmental Cell 11 3 2006 279 287 10.1016/j.devcel.2006.08.004
    • (2006) Developmental Cell , vol.11 , Issue.3 , pp. 279-287
    • Mogilner, A.1    Wollman, R.2    Marshall, W.F.3
  • 31
    • 70849098888 scopus 로고    scopus 로고
    • Actin, a central player in cell shape and movement
    • 10.1126/science.1175862
    • T.D. Pollard, and J.A. Cooper Actin, a central player in cell shape and movement Science (New York, N.Y.) 326 5957 2009 1208 1212 10.1126/science. 1175862
    • (2009) Science (New York, N.Y.) , vol.326 , Issue.5957 , pp. 1208-1212
    • Pollard, T.D.1    Cooper, J.A.2
  • 33
    • 79959677602 scopus 로고    scopus 로고
    • Life at the leading edge
    • 10.1016/j.cell.2011.06.010
    • A.J. Ridley Life at the leading edge Cell 145 7 2011 1012 1022 10.1016/j.cell.2011.06.010
    • (2011) Cell , vol.145 , Issue.7 , pp. 1012-1022
    • Ridley, A.J.1
  • 34
    • 44449134820 scopus 로고    scopus 로고
    • A practical guide to single-molecule FRET
    • 10.1038/nmeth.1208
    • R. Roy, S. Hohng, and T. Ha A practical guide to single-molecule FRET Nature Methods 5 6 2008 507 516 10.1038/nmeth.1208
    • (2008) Nature Methods , vol.5 , Issue.6 , pp. 507-516
    • Roy, R.1    Hohng, S.2    Ha, T.3
  • 36
    • 77954639410 scopus 로고    scopus 로고
    • Acidification of the oxygen scavenging system in single-molecule fluorescence studies: In situ sensing with a ratiometric dual-emission probe
    • 10.1021/ac1008749
    • X. Shi, J. Lim, and T. Ha Acidification of the oxygen scavenging system in single-molecule fluorescence studies: In situ sensing with a ratiometric dual-emission probe Analytical Chemistry 82 14 2010 6132 6138 10.1021/ac1008749
    • (2010) Analytical Chemistry , vol.82 , Issue.14 , pp. 6132-6138
    • Shi, X.1    Lim, J.2    Ha, T.3
  • 37
    • 33846656891 scopus 로고    scopus 로고
    • SnapShot: Actin regulators i
    • 10.1016/j.cell.2007.02.001
    • A.D. Siripala, and M.D. Welch SnapShot: Actin regulators I Cell 128 3 2007 626 10.1016/j.cell.2007.02.001
    • (2007) Cell , vol.128 , Issue.3 , pp. 626
    • Siripala, A.D.1    Welch, M.D.2
  • 39
    • 84884697646 scopus 로고    scopus 로고
    • Three-color single molecule imaging shows WASP detachment from Arp2/3 complex triggers actin filament branch formation
    • 10.7554/eLife.01008
    • B.A. Smith, S.B. Padrick, L.K. Doolittle, K. Daugherty-Clarke, I.R. Corrêa Jr., and M.Q. Xu et al. Three-color single molecule imaging shows WASP detachment from Arp2/3 complex triggers actin filament branch formation eLife 2 2013 e01008 10.7554/eLife.01008
    • (2013) ELife , vol.2 , pp. 01008
    • Smith, B.A.1    Padrick, S.B.2    Doolittle, L.K.3    Daugherty-Clarke, K.4    Corrêa, Jr.I.R.5    Xu, M.Q.6
  • 40
    • 79957453658 scopus 로고    scopus 로고
    • Cofilin tunes the nucleotide state of actin filaments and severs at bare and decorated segment boundaries
    • 10.1016/j.cub.2011.03.064
    • C. Suarez, J. Roland, R. Boujemaa-Paterski, H. Kang, B.R. McCullough, and A.C. Reymann et al. Cofilin tunes the nucleotide state of actin filaments and severs at bare and decorated segment boundaries Current Biology 21 10 2011 862 868 10.1016/j.cub.2011.03.064
    • (2011) Current Biology , vol.21 , Issue.10 , pp. 862-868
    • Suarez, C.1    Roland, J.2    Boujemaa-Paterski, R.3    Kang, H.4    McCullough, B.R.5    Reymann, A.C.6
  • 41
    • 0024991350 scopus 로고
    • Myosin step size. Estimation from slow sliding movement of actin over low densities of heavy meromyosin
    • 10.1016/0022-2836(90)90287-V
    • T.Q. Uyeda, S.J. Kron, and J.A. Spudich Myosin step size. Estimation from slow sliding movement of actin over low densities of heavy meromyosin Journal of Molecular Biology 214 3 1990 699 710 10.1016/0022-2836(90)90287-V
    • (1990) Journal of Molecular Biology , vol.214 , Issue.3 , pp. 699-710
    • Uyeda, T.Q.1    Kron, S.J.2    Spudich, J.A.3
  • 42
    • 84855304794 scopus 로고    scopus 로고
    • Clathrin-mediated endocytosis in budding yeast
    • 10.1016/j.tcb.2011.09.001
    • J. Weinberg, and D.G. Drubin Clathrin-mediated endocytosis in budding yeast Trends in Cell Biology 22 1 2012 1 13 10.1016/j.tcb.2011.09.001
    • (2012) Trends in Cell Biology , vol.22 , Issue.1 , pp. 1-13
    • Weinberg, J.1    Drubin, D.G.2
  • 43
    • 0021261156 scopus 로고
    • Direct observation of motion of single F-actin filaments in the presence of myosin
    • T. Yanagida, M. Nakase, K. Nishiyama, and F. Oosawa Direct observation of motion of single F-actin filaments in the presence of myosin Nature 307 5946 1984 58 60
    • (1984) Nature , vol.307 , Issue.5946 , pp. 58-60
    • Yanagida, T.1    Nakase, M.2    Nishiyama, K.3    Oosawa, F.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.