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Cited by 223Cellular Mechanics and InteractionsProtein Structure and DynamicsMicrotubule and mitosis dynamics

Cofilin Tunes the Nucleotide State of Actin Filaments and Severs at Bare and Decorated Segment Boundaries

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Suarez, Cristian, Roland, Jérémy, Boujemaa-Paterski, Rajaa, Kang, Hyeran, McCullough, Brannon R., Reymann, Anne-Cécile, Guérin, Christophe, Martiel, Jean-Louis +2 more·2011·Current Biology
DOI 10.1016/j.cub.2011.03.064PMC PMC3100394
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Abstract

Actin-based motility demands the spatial and temporal coordination of numerous regulatory actin-binding proteins (ABPs), many of which bind with affinities that depend on the nucleotide state of actin filament. Cofilin, one of three ABPs that precisely choreograph actin assembly and organization into comet tails that drive motility in vitro, binds and stochastically severs aged ADP actin filament segments of de novo growing actin filaments. Deficiencies in methodologies to track in real time the nucleotide state of actin filaments, as well as cofilin severing, limit the molecular understanding of coupling between actin filament chemical and mechanical states and severing. We engineered a fluorescently labeled cofilin that retains actin filament binding and severing activities. Because cofilin binding depends strongly on the actin-bound nucleotide, direct visualization of fluorescent cofilin binding serves as a marker of the actin filament nucleotide state during assembly. Bound cofilin allosterically accelerates P(i) release from unoccupied filament subunits, which shortens the filament ATP/ADP-P(i) cap length by nearly an order of magnitude. Real-time visualization of filament severing indicates that fragmentation scales with and occurs preferentially at boundaries between bare and cofilin-decorated filament segments, thereby controlling the overall filament length, depending on cofilin binding density.

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  • Cofilin binds to F-actin with a Kd < 0.05 μM and results in disassembly of F-actin.

    “One of these binding partners is cofilin, a 21 kDa eukaryotic protein, which binds to F-actin with a K d < 0.05 µM33 and results in disassembly of F-actin34, 35.”

    From Multivalent cross-linking of actin filaments and microtubules through the microtubule-associated protein Tau (2017) · cites this paper as [35]

    Citation 33 is attached to the Kd claim. In Results and Discussion (‘Bound ADF/cofilin dissociates slowly from actin filaments’; page unavailable), the paper reports rapid binding to bare actin filaments and high overall binding affinity, but gives no Kd below 0.05 µM. The disassembly clause is assigned to citations 34 and 35, not this source. (LLM, conf=0.84)

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Research works printed but not linked: 31

  1. [1]Pollard TD Blanchoin L Mullins RD 2000 Molecular Mechanisms Controlling Actin Filament Dynamics in Nonmuscle Cells Annu Rev Biophys 29 545 576 10940259
  2. [2]Loisel TP Boujemaa R Pantaloni D Carlier MF 1999 Reconstitution of actin-based motility of Listeria and Shigella using pure proteins Nature 401 613 616 10524632
  3. [3]Michelot A Berro J Guerin C Boujemaa-Paterski R Staiger CJ Martiel JL Blanchoin L 2007 Actin-filament stochastic dynamics mediated by ADF/cofilin Curr Biol 17 825 833 17493813
  4. [4]Lappalainen P Fedorov EV Fedorov AA Almo SC Drubin DG 1997 Essential functions and actin-binding surfaces of yeast cofilin revealed by systematic mutagenesis EMBO J 16 5520 5530 9312011 PMC1170184
  5. [5]Blanchoin L Pollard TD 1999 Mechanism of interaction of Acanthamoeba actophorin (ADF/cofilin) with actin filaments J Biol Chem 274 15538 15546 10336448
  6. [6]Achard V Martiel JL Michelot A Guerin C Reymann AC Blanchoin L Boujemaa-Paterski R A “primer”-based mechanism underlies branched actin filament network formation and motility Curr Biol 20 423 428 20188562
  7. [7]Bobkov AA Muhlrad A Kokabi K Vorobiev S Almo SC Reisler E 2002 Structural effects of cofilin on longitudinal contacts in F-actin J Mol Biol 323 739 750 12419261
  8. [8]Vavylonis D Yang Q O’Shaughnessy B 2005 Actin polymerization kinetics, cap structure, and fluctuations Proc Natl Acad Sci USA 102 8543 8548 15939882 PMC1150824
  9. [9]Roland J Berro J Michelot A Blanchoin L Martiel JL 2007 Stochastic severing of actin filaments by ADF/cofilin controls the emergence of a steady dynamical regime Biophys J 94 2082 2094 18065447 PMC2257902
  10. [10]Chan C Beltzner CC Pollard TD 2009 Cofilin dissociates Arp2/3 complex and branches from actin filaments Curr Biol 19 537 545 19362000 PMC3711486
  11. [11]Cao W Goodarzi JP De La Cruz EM 2006 Energetics and kinetics of cooperative cofilin-actin filament interactions J Mol Biol 361 257 267 16843490
  12. [12]De La Cruz EM Sept D 2010 The kinetics of cooperative cofilin binding reveals two states of the cofilin-actin filament Biophys J 98 1893 1901 20441753 PMC2862197
  13. [13]Prochniewicz E Janson N Thomas DD De la Cruz EM 2005 Cofilin increases the torsional flexibility and dynamics of actin filaments J Mol Biol 353 990 1000 16213521
  14. [14]De La Cruz EM 2009 How cofilin severs an actin filament Biophys Rev 1 51 59 20700473 PMC2917815
  15. [15]McGough A Pope B Chiu W Weeds A 1997 Cofilin changes the twist of F-actin: implications for actin filament dynamics and cellular function J Cell Biol 138 771 781 9265645 PMC2138052
  16. [16]Galkin VE Orlova A Lukoyanova N Wriggers W Egelman EH 2001 Actin depolymerizing factor stabilizes an existing state of F-actin and can change the tilt of F-actin subunits J Cell Biol 153 75 86 11285275 PMC2185532
  17. [17]Muhlrad A Kudryashov D Michael Peyser Y Bobkov AA Almo SC Reisler E 2004 Cofilin induced conformational changes in F-actin expose subdomain 2 to proteolysis J Mol Biol 342 1559 1567 15364581
  18. [18]Pfaendtner J De La Cruz EM Voth GA 2010 Actin filament remodeling by actin depolymerization factor/cofilin Proc Natl Acad Sci USA 107 7299 7304 20368459 PMC2867716
  19. [19]McCullough BR Blanchoin L Martiel JL De la Cruz EM 2008 Cofilin increases the bending flexibility of actin filaments: implications for severing and cell mechanics J Mol Biol 381 550 558 18617188 PMC2753234
  20. [20]De La Cruz EM 2005 Cofilin binding to muscle and non-muscle actin filaments: isoform-dependent cooperative interactions J Mol Biol 346 557 564 15670604
  21. [21]Bobkov AA Muhlrad A Pavlov DA Kokabi K Yilmaz A Reisler E 2006 Cooperative effects of cofilin (ADF) on actin structure suggest allosteric mechanism of cofilin function J Mol Biol 356 325 334 16375920
  22. [22]Dedova IV Nikolaeva OP Safer D De La Cruz EM dos Remedios CG 2006 Thymosin beta4 induces a conformational change in actin monomers Biophys J 90 985 992 16272441 PMC1367123
  23. [23]Blanchoin L Pollard TD 2002 Hydrolysis of bound ATP by polymerized actin depends on the bound divalent cation but not profilin Biochemistry 41 597 602 11781099
  24. [24]Ti SC Pollard TD 2011 Purification of actin from fission yeast Schizosaccharomyces pombe and characterization of functional differences from muscle actin J Biol Chem 286 5784 5792 21148484 PMC3037691
  25. [25]Svitkina TM Borisy GG 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 10352018 PMC2133125
  26. [26]Iwasa JH Mullins RD 2007 Spatial and Temporal Relationships between Actin-Filament Nucleation, Capping, and Disassembly Curr Biol 17 395 406 17331727 PMC3077992
  27. [27]Okreglak V Drubin DG 2007 Cofilin recruitment and function during actin-mediated endocytosis dictated by actin nucleotide state J Cell Biol 178 1251 1264 17875745 PMC2064657
  28. [28]Ressad F Didry D Xia GX Hong Y Chua NH Pantaloni D Carlier MF 1998 Kinetic analysis of the interaction of actin-depolymerizing factor (ADF)/cofilin with G- and F-actins. Comparison of plant and human ADFs and effect of phosphorylation J Biol Chem 273 20894 20902 9694836
  29. [29]Andrianantoandro E Pollard TD 2006 Mechanism of actin filament turnover by severing and nucleation at different concentrations of ADF/cofilin Mol Cell 24 13 23 17018289
  30. [30]Pavlov D Muhlrad A Cooper J Wear M Reisler E 2007 Actin filament severing by cofilin J Mol Biol 365 1350 1358 17134718 PMC2572264
  31. [31]Kueh HY Charras GT Mitchison TJ Brieher WM 2008 Actin disassembly by cofilin, coronin, and Aip1 occurs in bursts and is inhibited by barbed-end cappers J Cell Biol 182 341 353 18663144 PMC2483518

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Authors
Suarez, C., Roland, J., Boujemaa-Paterski, R., Kang, H., McCullough, B. R., Reymann, A.-C., Guérin, C., Martiel, J.-L., De La Cruz, E. M., & Blanchoin, L.
Affiliations
  • Centre National de la Recherche Scientifique (FR)
  • Yale University (US)
Corresponding author
Blanchoin, Laurent
ORCID
Venue
Current Biology
Publisher
Elsevier BV
Published
2011-05
Volume
21
Issue
10
Pages
862-868
ISSN
0960-9822 (ISSN-L)
DOI
10.1016/j.cub.2011.03.064
PMC
PMC3100394
OpenAlex
W2033926605
Cited by
223
References
0
Citations by year
2026: 11 · 2025: 17 · 2024: 14 · 2023: 15 · 2022: 14 · 2021: 13 · 2020: 14 · 2019: 19 · 2018: 13 · 2017: 14 · 2016: 14 · 2015: 21 · 2014: 14 · 2013: 13 · 2012: 8
FWCI
6.35
Type
journal article
Language
en
Update notices
erratum (2011-05-24)
Open access
Licence
Locations
  • Current Biology (publishedVersion)
  • PubMed (publishedVersion)
  • Europe PMC (PubMed Central) (acceptedVersion)
  • PubMed Central (acceptedVersion)
  • HAL (submittedVersion, other-oa)
Funders
  • Agence Nationale de la Recherche (ANR-08-SYSC-0013)
  • National Institute of General Medical Sciences (R01GM071688, GM071688)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular Mechanics and Interactions
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
Keywords
cofilin, actin filament severing, actin-binding proteins, actin filament assembly, phosphate release, filament fragmentation, actin-based motility, real-time imaging
MeSH terms
Actins, Escherichia coli, Image Processing, Computer-Assisted, Microscopy, Fluorescence, Models, Biological, Movement, Nucleotides, Saccharomyces cerevisiae, Protein Engineering, Least-Squares Analysis, Saccharomyces cerevisiae Proteins, Cofilin 1

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