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Volumn 101, Issue 4, 2011, Pages 803-808

Fragmentation is crucial for the steady-state dynamics of actin filaments

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; PHOSPHATE;

EID: 80052499090     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2011.07.009     Document Type: Article
Times cited : (16)

References (31)
  • 1
    • 34548160002 scopus 로고    scopus 로고
    • Control of actin assembly dynamics in cell motility
    • DOI 10.1074/jbc.R700020200
    • M.F. Carlier, and D. Pantaloni Control of actin assembly dynamics in cell motility J. Biol. Chem. 282 2007 23005 23009 (Pubitemid 47311896)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.32 , pp. 23005-23009
    • Carlier, M.-F.1    Pantaloni, D.2
  • 2
    • 0033533789 scopus 로고    scopus 로고
    • Reconstitution of actin-based motility of Listeria and Shigella using pure proteins
    • T.P. Loisel, and R. Boujemaa M.F. Carlier 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    Carlier, M.F.3
  • 4
    • 0017176529 scopus 로고
    • Head to tail polymerization of actin
    • A. Wegner Head to tail polymerization of actin J. Mol. Biol. 108 1976 139 150
    • (1976) J. Mol. Biol. , vol.108 , pp. 139-150
    • Wegner, A.1
  • 5
    • 0019495845 scopus 로고
    • Direct measurement of actin polymerization rate constants by electron microscopy of actin filaments nucleated by isolated microvillus cores
    • DOI 10.1083/jcb.88.3.654
    • T.D. Pollard, and M.S. Mooseker Direct measurement of actin polymerization rate constants by electron microscopy of actin filaments nucleated by isolated microvillus cores J. Cell Biol. 88 1981 654 659 (Pubitemid 11097958)
    • (1981) Journal of Cell Biology , vol.88 , Issue.3 , pp. 654-659
    • Pollard, T.D.1    Mooseker, M.S.2
  • 6
    • 0022881322 scopus 로고
    • Rate constants for the reactions of ATP- and ADP-actin with the ends of actin filaments
    • DOI 10.1083/jcb.103.6.2747
    • T.D. Pollard Rate constants for the reactions of ATP- and ADP-actin with the ends of actin filaments J. Cell Biol. 103 1986 2747 2754 (Pubitemid 17008020)
    • (1986) Journal of Cell Biology , vol.103 , Issue.6 , pp. 2747-2754
    • Pollard, T.D.1
  • 7
    • 0019820715 scopus 로고
    • Requirement of divalent cations for fast exchange of actin monomers and actin filament subunits
    • A. Wegner, and J.-M. Neuhaus Requirement of divalent cations for fast exchange of actin monomers and actin filament subunits J. Mol. Biol. 153 1981 681 693 (Pubitemid 12180294)
    • (1981) Journal of Molecular Biology , vol.153 , Issue.3 , pp. 681-693
    • Wegner, A.1    Neuhaus, J.M.2
  • 8
    • 0019971945 scopus 로고
    • Actin filaments undergo limited subunit exchange in physiological salt conditions
    • DOI 10.1083/jcb.94.2.316
    • J.D. Pardee, and P.A. Simpson J.A. Spudich Actin filaments undergo limited subunit exchange in physiological salt conditions J. Cell Biol. 94 1982 316 324 (Pubitemid 12026779)
    • (1982) Journal of Cell Biology , vol.94 , Issue.2 , pp. 316-324
    • Pardee, J.D.1    Simpson, P.A.2    Stryer, L.3    Spudich, J.A.4
  • 10
    • 0001360883 scopus 로고
    • Dephosphorylation of adenosine triphosphate in actin solutions at low concentrations of magnesium
    • S. Asakura, and F. Oosawa Dephosphorylation of adenosine triphosphate in actin solutions at low concentrations of magnesium Arch. Biochem. Biophys. 87 1960 273 280
    • (1960) Arch. Biochem. Biophys. , vol.87 , pp. 273-280
    • Asakura, S.1    Oosawa, F.2
  • 11
    • 0023637721 scopus 로고
    • Actin polymerization and ATP hydrolysis
    • E.D. Korn, M.-F. Carlier, and D. Pantaloni Actin polymerization and ATP hydrolysis Science 238 1987 638 644 (Pubitemid 17158293)
    • (1987) Science , vol.238 , Issue.4827 , pp. 638-644
    • Korn, E.D.1    Carlier, M.-F.2    Pantaloni, D.3
  • 12
    • 0036713779 scopus 로고    scopus 로고
    • Microscopic analysis of polymerization dynamics with individual actin filaments
    • DOI 10.1038/ncb841
    • I. Fujiwara, and S. Takahashi S. Ishiwata Microscopic analysis of polymerization dynamics with individual actin filaments Nat. Cell Biol. 4 2002 666 673 (Pubitemid 34993702)
    • (2002) Nature Cell Biology , vol.4 , Issue.9 , pp. 666-673
    • Fujiwara, I.1    Takahashi, S.2    Tadakuma, H.3    Funatsu, T.4    Ishiwata, S.5
  • 13
    • 18844389128 scopus 로고    scopus 로고
    • Real-time measurements of actin filament polymerization by total internal reflection fluorescence microscopy
    • DOI 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 Biophys. J. 88 2005 1387 1402 (Pubitemid 40975966)
    • (2005) Biophysical Journal , vol.88 , Issue.2 , pp. 1387-1402
    • Kuhn, J.R.1    Pollard, T.D.2
  • 16
    • 69249088090 scopus 로고    scopus 로고
    • Structural plasticity in actin and tubulin polymer dynamics
    • H.Y. Kueh, and T.J. Mitchison Structural plasticity in actin and tubulin polymer dynamics Science 325 2009 960 963
    • (2009) Science , vol.325 , pp. 960-963
    • Kueh, H.Y.1    Mitchison, T.J.2
  • 17
    • 77952896939 scopus 로고    scopus 로고
    • Control of actin filament treadmilling in cell motility
    • B. Bugyi, and M.-F. Carlier Control of actin filament treadmilling in cell motility Annu Rev Biophys. 39 2010 449 470
    • (2010) Annu Rev Biophys. , vol.39 , pp. 449-470
    • Bugyi, B.1    Carlier, M.-F.2
  • 18
    • 0019968097 scopus 로고
    • Spontaneous fragmentation of actin filaments in physiological conditions
    • DOI 10.1038/296266a0
    • A. Wegner Spontaneous fragmentation of actin filaments in physiological conditions Nature 296 1982 266 267 (Pubitemid 12072147)
    • (1982) Nature , vol.296 , Issue.5854 , pp. 266-267
    • Wegner, A.1
  • 19
    • 0024511257 scopus 로고
    • Co-operativity in protein-protein association. The structure and stability of the actin filament
    • DOI 10.1016/0022-2836(89)90494-4
    • H.P. Erickson Co-operativity in protein-protein association. The structure and stability of the actin filament J. Mol. Biol. 206 1989 465 474 (Pubitemid 19104986)
    • (1989) Journal of Molecular Biology , vol.206 , Issue.3 , pp. 465-474
    • Erickson, H.P.1
  • 20
    • 0032796310 scopus 로고    scopus 로고
    • Annealing accounts for the length of actin filaments formed by spontaneous polymerization
    • D. Sept, and J. Xu J.A. McCammon Annealing accounts for the length of actin filaments formed by spontaneous polymerization Biophys. J. 77 1999 2911 2919
    • (1999) Biophys. J. , vol.77 , pp. 2911-2919
    • Sept, D.1    Xu, J.2    McCammon, J.A.3
  • 21
    • 41949132039 scopus 로고    scopus 로고
    • Stochastic simulation of actin dynamics reveals the role of annealing and fragmentation
    • J. Fass, and C. Pak A. Mogilner Stochastic simulation of actin dynamics reveals the role of annealing and fragmentation J. Theor. Biol. 252 2008 173 183
    • (2008) J. Theor. Biol. , vol.252 , pp. 173-183
    • Fass, J.1    Pak, C.2    Mogilner, A.3
  • 22
    • 77955615646 scopus 로고    scopus 로고
    • Mathematical modeling of endocytic actin patch kinetics in fission yeast: Disassembly requires release of actin filament fragments
    • J. Berro, V. Sirotkin, and T.D. Pollard Mathematical modeling of endocytic actin patch kinetics in fission yeast: disassembly requires release of actin filament fragments Mol. Biol. Cell 21 2010 2905 2915
    • (2010) Mol. Biol. Cell , vol.21 , pp. 2905-2915
    • Berro, J.1    Sirotkin, V.2    Pollard, T.D.3
  • 23
    • 0015218407 scopus 로고
    • The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin
    • J.A. Spudich, and S. Watt The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin J. Biol. Chem. 246 1971 4866 4871
    • (1971) J. Biol. Chem. , vol.246 , pp. 4866-4871
    • Spudich, J.A.1    Watt, S.2
  • 24
    • 78751584808 scopus 로고    scopus 로고
    • Slow down of actin depolymerization by cross-linking molecules
    • K.M. Schmoller, C. Semmrich, and A.R. Bausch Slow down of actin depolymerization by cross-linking molecules J. Struct. Biol. 173 2011 350 357
    • (2011) J. Struct. Biol. , vol.173 , pp. 350-357
    • Schmoller, K.M.1    Semmrich, C.2    Bausch, A.R.3
  • 25
    • 0026684153 scopus 로고
    • A continuous spectrophotometric assay for inorganic phosphate and for measuring phosphate release kinetics in biological systems
    • M.R. Webb A continuous spectrophotometric assay for inorganic phosphate and for measuring phosphate release kinetics in biological systems Proc. Natl. Acad. Sci. USA 89 1992 4884 4887
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 4884-4887
    • Webb, M.R.1
  • 26
    • 0014755321 scopus 로고
    • Electron microscopic particle length of F-actin polymerized in vitro
    • M. Kawamura, and K. Maruyama Electron microscopic particle length of F-actin polymerized in vitro J. Biochem. 67 1970 437 457
    • (1970) J. Biochem. , vol.67 , pp. 437-457
    • Kawamura, M.1    Maruyama, K.2
  • 27
    • 0027378260 scopus 로고
    • Actin filament annealing in the presence of ATP and phalloidin
    • DOI 10.1021/bi00097a011
    • H.J. Kinosian, and L.A. Selden L.C. Gershman Actin filament annealing in the presence of ATP and phalloidin Biochemistry 32 1993 12353 12357 (Pubitemid 23357954)
    • (1993) Biochemistry , vol.32 , Issue.46 , pp. 12353-12357
    • Kinosian, H.J.1    Selden, L.A.2    Estes, J.E.3    Gershman, L.C.4
  • 28
    • 0029661920 scopus 로고    scopus 로고
    • Continuous monitoring of P(i) release following nucleotide hydrolysis in actin or tubulin assembly using 2-amino-6-mercapto-7-methylpurine ribonucleoside and purine-nucleoside phosphorylase as an enzyme-linked assay
    • DOI 10.1021/bi961325o
    • R. Melki, S. Fievez, and M.F. Carlier Continuous monitoring of Pi release following nucleotide hydrolysis in actin or tubulin assembly using 2-amino-6-mercapto-7-methylpurine ribonucleoside and purine-nucleoside phosphorylase as an enzyme-linked assay Biochemistry 35 1996 12038 12045 (Pubitemid 26313674)
    • (1996) Biochemistry , vol.35 , Issue.37 , pp. 12038-12045
    • Melki, R.1    Fievez, S.2    Carlier, M.-F.3
  • 29
    • 0027418763 scopus 로고
    • Nucleotide binding to actin. Cation dependence of nucleotide dissociation and exchange rates
    • H.J. Kinosian, and L.A. Selden L.C. Gersham Nuceotide binding to actin. Cation dependence of nucleotide dissociation and exchange rates J. Biol. Chem. 268 1993 8683 8691 (Pubitemid 23118654)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.12 , pp. 8683-8691
    • Kinosian, H.J.1    Selden, L.A.2    Estes, J.E.3    Gershman, L.C.4
  • 30
    • 0022509325 scopus 로고
    • Kinetics of actin depolymerization: Influence of ions, temperature, age of F-actin, cytochalasin B and phalloidin
    • DOI 10.1016/0167-4838(86)90088-9
    • H. Wendel, and P. Dancker Kinetics of actin depolymerization: influence of ions, temperature, age of F-actin, cytochalasin B and phalloidin Biochim. Biophys. Acta 873 1986 387 396 (Pubitemid 16002292)
    • (1986) Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology , vol.873 , Issue.3 , pp. 387-396
    • Wendel, H.1    Dancker, P.2
  • 31
    • 60849130414 scopus 로고    scopus 로고
    • Actin filament dynamics are dominated by rapid growth and severing activity in the Arabidopsis cortical array
    • C.J. Staiger, and M.B. Sheahan L. Blanchoin Actin filament dynamics are dominated by rapid growth and severing activity in the Arabidopsis cortical array J. Cell Biol. 184 2009 269 280
    • (2009) J. Cell Biol. , vol.184 , pp. 269-280
    • Staiger, C.J.1    Sheahan, M.B.2    Blanchoin, L.3


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