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PMID: 11285275 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Actin depolymerizing factor stabilizes an existing state of F-actin and can change the tilt of F-actin subunits.

The Journal of cell biology ·Vol. 153 ·No. 1 ·2001-04-02 ·Pages 75-86

Galkin VE, Orlova A, Lukoyanova N, Wriggers W, Egelman EH

Abstract

Proteins in the actin depolymerizing factor (ADF)/cofilin family are essential for rapid F-actin turnover, and most depolymerize actin in a pH-dependent manner. Complexes of human and plant ADF with F-actin at different pH were examined using electron microscopy and a novel method of image analysis for helical filaments. Although ADF changes the mean twist of actin, we show that it does this by stabilizing a preexisting F-actin angular conformation. In addition, ADF induces a large ( approximately 12 degrees ) tilt of actin subunits at high pH where filaments are readily disrupted. A second ADF molecule binds to a site on the opposite side of F-actin from that of the previously described ADF binding site, and this second site is only largely occupied at high pH. All of these states display a high degree of cooperativity that appears to be an integral part of F-actin.

MeSH Terms
Actin Depolymerizing Factors Actins/chemistry,metabolism Animals Destrin Humans Microfilament Proteins/chemistry,metabolism Models, Molecular Rabbits
Chemicals
Actin Depolymerizing Factors Actins DSTN protein, human Destrin Microfilament Proteins
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Galkin V E
Department of Biochemistry and Molecular Genetics, University of Virginia Health Sciences Center, Charlottesville, Virginia 22908, USA.
Orlova A
Lukoyanova N
Wriggers W
Egelman E H
References (54)
54 references, click to expand
  1. Two activities of cofilin, severing and accelerating directional depolymerization of actin filaments, are affected differentially by mutations around the actin-binding helix.
    EMBO J. 1999 Dec 1;18(23):6752-61 PMID: 10581248
  2. Cooperative rigor binding of myosin to actin is a function of F-actin structure.
    J Mol Biol. 1997 Feb 7;265(5):469-74 PMID: 9048941
  3. Regulating actin-filament dynamics in vivo.
    Trends Biochem Sci. 2000 Jan;25(1):19-23 PMID: 10637608
  4. F-actin retains a memory of angular order.
    Biophys J. 2000 Apr;78(4):2180-5 PMID: 10733996
  5. Accelerating on a treadmill: ADF/cofilin promotes rapid actin filament turnover in the dynamic cytoskeleton.
    J Cell Biol. 1997 Mar 24;136(6):1165-8 PMID: 9087434
  6. Actin depolymerizing factor (ADF/cofilin) enhances the rate of filament turnover: implication in actin-based motility.
    J Cell Biol. 1997 Mar 24;136(6):1307-22 PMID: 9087445
  7. Control of actin dynamics in cell motility.
    J Mol Biol. 1997 Jun 20;269(4):459-67 PMID: 9217250
  8. Cofilin changes the twist of F-actin: implications for actin filament dynamics and cellular function.
    J Cell Biol. 1997 Aug 25;138(4):771-81 PMID: 9265645
  9. Essential functions and actin-binding surfaces of yeast cofilin revealed by systematic mutagenesis.
    EMBO J. 1997 Sep 15;16(18):5520-30 PMID: 9312011
  10. Analogous F-actin binding by cofilin and gelsolin segment 2 substantiates their structural relationship.
    J Biol Chem. 1997 Dec 26;272(52):32750-8 PMID: 9407048
  11. Uncoupling actin filament fragmentation by cofilin from increased subunit turnover.
    J Mol Biol. 2000 May 12;298(4):649-61 PMID: 10788327
  12. Molecular mechanisms controlling actin filament dynamics in nonmuscle cells.
    Annu Rev Biophys Biomol Struct. 2000;29:545-76 PMID: 10940259
  13. Intracellular pH modulation of ADF/cofilin proteins.
    Cell Motil Cytoskeleton. 2000 Dec;47(4):319-36 PMID: 11093252
  14. A robust algorithm for the reconstruction of helical filaments using single-particle methods.
    Ultramicroscopy. 2000 Dec;85(4):225-34 PMID: 11125866
  15. Using situs for flexible and rigid-body fitting of multiresolution single-molecule data.
    J Struct Biol. 2001 Feb-Mar;133(2-3):193-202 PMID: 11472090
  16. Chicken-gizzard actin: polymerization and stability.
    Eur J Biochem. 1980 Feb;104(1):41-52 PMID: 6445264
  17. F-actin is a helix with a random variable twist.
    Nature. 1982 Jul 8;298(5870):131-5 PMID: 7201078
  18. The correlation averaging of a regularly arranged bacterial cell envelope protein.
    J Microsc. 1982 Aug;127(Pt 2):127-38 PMID: 7120365
  19. Actin filaments, stereocilia, and hair cells of the bird cochlea. II. Packing of actin filaments in the stereocilia and in the cuticular plate and what happens to the organization when the stereocilia are bent.
    J Cell Biol. 1983 Mar;96(3):822-34 PMID: 6682111
  20. pH control of actin polymerization by cofilin.
    J Biol Chem. 1985 Nov 25;260(27):14410-2 PMID: 4055781
  21. Purification and characterization of actophorin, a new 15,000-dalton actin-binding protein from Acanthamoeba castellanii.
    J Biol Chem. 1986 Jan 5;261(1):477-85 PMID: 3941084
  22. Improved method for mapping the binding site of an actin-binding protein in the actin sequence. Use of a site-directed antibody against the N-terminal region of actin as a probe of its N-terminus.
    Biochemistry. 1986 Oct 7;25(20):6186-92 PMID: 3790514
  23. End-label fingerprintings show that an N-terminal segment of depactin participates in interaction with actin.
    Biochemistry. 1989 Jan 10;28(1):102-6 PMID: 2706236
  24. Subtilisin cleavage of actin inhibits in vitro sliding movement of actin filaments over myosin.
    J Cell Biol. 1990 Aug;111(2):465-70 PMID: 2143196
  25. Atomic model of the actin filament.
    Nature. 1990 Sep 6;347(6288):44-9 PMID: 2395461
  26. Alteration in crossbridge kinetics caused by mutations in actin.
    Nature. 1990 Nov 29;348(6300):440-2 PMID: 2123302
  27. Inhibition of sliding movement of F-actin by crosslinking emphasizes the role of actin structure in the mechanism of motility.
    J Mol Biol. 1990 Dec 5;216(3):761-72 PMID: 2147958
  28. Supercoiling of f-actin filaments.
    J Struct Biol. 1990 May;103(3):225-31 PMID: 2261308
  29. Inhibition of actin polymerization by a synthetic dodecapeptide patterned on the sequence around the actin-binding site of cofilin.
    J Biol Chem. 1991 Jun 5;266(16):10485-9 PMID: 2037594
  30. Characterization of actin filament severing by actophorin from Acanthamoeba castellanii.
    J Cell Biol. 1991 Dec;115(6):1611-20 PMID: 1757465
  31. Human actin depolymerizing factor mediates a pH-sensitive destruction of actin filaments.
    Biochemistry. 1993 Sep 28;32(38):9985-93 PMID: 8399167
  32. Analysis of the interactions of actin depolymerizing factor with G- and F-actin.
    Biochemistry. 1993 Sep 28;32(38):9994-10004 PMID: 8399168
  33. A 13-A map of the actin-scruin filament from the limulus acrosomal process.
    J Cell Biol. 1993 Oct;123(2):337-44 PMID: 8408217
  34. Structural dynamics of F-actin: I. Changes in the C terminus.
    J Mol Biol. 1995 Feb 3;245(5):582-97 PMID: 7844828
  35. Control of actin dynamics.
    Curr Opin Cell Biol. 1998 Feb;10(1):45-51 PMID: 9484594
  36. 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. 1998 Aug 14;273(33):20894-902 PMID: 9694836
  37. Kinetic studies on the effect of yeast cofilin on yeast actin polymerization.
    Biochemistry. 1998 Sep 22;37(38):13276-84 PMID: 9748335
  38. The effect of two actin depolymerizing factors (ADF/cofilins) on actin filament turnover: pH sensitivity of F-actin binding by human ADF, but not of Acanthamoeba actophorin.
    Eur J Biochem. 1998 Sep 1;256(2):388-97 PMID: 9760179
  39. Self-organizing neural networks bridge the biomolecular resolution gap.
    J Mol Biol. 1998 Dec 18;284(5):1247-54 PMID: 9878345
  40. Intrastrand cross-linked actin between Gln-41 and Cys-374. III. Inhibition of motion and force generation with myosin.
    Biochemistry. 1998 Dec 22;37(51):17801-9 PMID: 9922146
  41. Investigating a back door mechanism of actin phosphate release by steered molecular dynamics.
    Proteins. 1999 May 1;35(2):262-73 PMID: 10223297
  42. Situs: A package for docking crystal structures into low-resolution maps from electron microscopy.
    J Struct Biol. 1999 Apr-May;125(2-3):185-95 PMID: 10222274
  43. UNC-60B, an ADF/cofilin family protein, is required for proper assembly of actin into myofibrils in Caenorhabditis elegans body wall muscle.
    J Cell Biol. 1999 May 3;145(3):491-502 PMID: 10225951
  44. Mechanism of interaction of Acanthamoeba actophorin (ADF/Cofilin) with actin filaments.
    J Biol Chem. 1999 May 28;274(22):15538-46 PMID: 10336448
  45. Aip1p interacts with cofilin to disassemble actin filaments.
    J Cell Biol. 1999 Jun 14;145(6):1251-64 PMID: 10366597
  46. ADF/cofilin weakens lateral contacts in the actin filament.
    J Mol Biol. 1999 Aug 20;291(3):513-9 PMID: 10448032
  47. Putting a new twist on actin: ADF/cofilins modulate actin dynamics.
    Trends Cell Biol. 1999 Sep;9(9):364-70 PMID: 10461190
  48. The identification of a second cofilin binding site on actin suggests a novel, intercalated arrangement of F-actin binding.
    J Biol Chem. 1999 Oct 8;274(41):28893-9 PMID: 10506133
  49. Structural dynamics of F-actin: II. Cooperativity in structural transitions.
    J Mol Biol. 1995 Feb 3;245(5):598-607 PMID: 7844829
  50. X-ray diffraction measurements of the extensibility of actin and myosin filaments in contracting muscle.
    Biophys J. 1994 Dec;67(6):2411-21 PMID: 7696481
  51. X-ray diffraction evidence for the extensibility of actin and myosin filaments during muscle contraction.
    Biophys J. 1994 Dec;67(6):2422-35 PMID: 7779179
  52. Tertiary structure of destrin and structural similarity between two actin-regulating protein families.
    Cell. 1996 Jun 28;85(7):1047-55 PMID: 8674111
  53. VMD: visual molecular dynamics.
    J Mol Graph. 1996 Feb;14(1):33-8, 27-8 PMID: 8744570
  54. Proteins of the ADF/cofilin family: essential regulators of actin dynamics.
    Annu Rev Cell Dev Biol. 1999;15:185-230 PMID: 10611961
Article Info
Journal
The Journal of cell biology
Abbr.
J Cell Biol
ISSN
0021-9525
DOI
10.1083/jcb.153.1.75
Published
2001-04-02
Pages
75-86
Language
English
Region
United States
NLM ID
0375356
PMCID
PMC2185532
Subset
IM
Grants
NCRR NIH HHS · P41-RR12255 · United States
NIAMS NIH HHS · R01-AR42023 · United States
External Links
PubMed source DOI: 10.1083/jcb.153.1.75 PMC Full Text View journal details
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