Actin Filament Severing by Cofilin

Journal of Molecular Biology

Volumn 365, Issue 5, 2007, Pages 1350-1358

  Pavlov, Dmitry ^a   Muhlrad, Andras ^b   Cooper, John ^c   Wear, Martin ^c   Reisler, Emil ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b HEBREW UNIVERSITY OF JERUSALEM   (Israel)

^c WASHINGTON UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

actin; cofilin; flexibility; gelsolin; severing

Indexed keywords

COFILIN; F ACTIN; GELSOLIN;

ACTIN FILAMENT; ARTICLE; CELL MOTILITY; CELL VIABILITY; DEPOLYMERIZATION; FLUORESCENCE MICROSCOPY; PRIORITY JOURNAL; PROTEIN POLYMERIZATION; PROTEIN STABILITY;

EID: 33846015786     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2006.10.102     Document Type: Article

References (44)

1. Pollard T.D., and Earnshaw W.C. Cell Biology (2004), Saunders, Philadelphia, PA
2. Lauffenburger D.A., and Horwitz A.F. Cell migration: a physically integrated molecular process. Cell 84 (1996) 359-369
3. Ghosh M., Ichetovkin I., Song X., Condeelis J.S., and Lawrence D.S. A new strategy for caging proteins regulated by kinases. J. Am. Chem. Soc. 124 (2002) 2440-2441
4. Ichetovkin I., Han J., Pang K.M., Knecht D.A., and Condeelis J.S. Actin filaments are severed by both native and recombinant dictyostelium cofilin but to different extents. Cell Motil. Cytoskel. 45 (2000) 293-306
5. Maciver S.K., Pope B.J., Whytock S., and Weeds A.G. 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. 256 (1998) 388-397
6. Carlier M.F., Laurent V., Santolini J., Melki R., Didry D., Xia G.X., et al. Actin depolymerizing factor (ADF/cofilin) enhances the rate of filament turnover: implication in actin-based motility. J. Cell Biol. 136 (1997) 1307-1322
7. Ono K., Parast M., Alberico C., Benian G.M., and Ono S. Specific requirement for two ADF/cofilin isoforms in distinct actin-dependent processes in Caenorhabditis elegans. J.Cell Sci. 116 (2003) 2073-2085
8. Ono S. Regulation of actin filament dynamics by actin depolymerizing factor/cofilin and actin-interacting protein 1: new blades for twisted filaments. Biochemistry 42 (2003) 13363-13370
9. Loisel T.P., Boujemaa R., Pantaloni D., and Carlier M.F. Reconstitution of actin-based motility of Listeria and Shigella using pure proteins. Nature 401 (1999) 613-616
10. Yap C.T., Simpson T.I., Pratt T., Price D.J., and Maciver S.K. The motility of glioblastoma tumour cells is modulated by intracellular cofilin expression in a concentration-dependent manner. Cell Motil. Cytoskel. 60 (2005) 153-165
11. Pope B.J., Gonsior S.M., Yeoh S., McGough A., and Weeds A.G. Uncoupling actin filament fragmentation by cofilin from increased subunit turnover. J. Mol. Biol. 298 (2000) 649-661
12. McGough A., Pope B., Chiu W., and Weeds A. Cofilin changes the twist of F-actin: implications for actin filament dynamics and cellular function. J. Cell Biol. 138 (1997) 771-781
13. Galkin V.E., Orlova A., Lukoyanova N., Wriggers W., and Egelman E.H. Actin depolymerizing factor stabilizes an existing state of F-actin and can change the tilt of F-actin subunits. J. Cell Biol. 153 (2001) 75-86
14. Sept D., Xu J., Pollard T.D., and McCammon J.A. Annealing accounts for the length of actin filaments formed by spontaneous polymerization. Biophys. J. 77 (1999) 2911-2919
15. Dedova I.V., Nikolaeva O.P., Mikhailova V.V., dos Remedios C.G., and Levitsky D.I. Two opposite effects of cofilin on the thermal unfolding of F-actin: a differential scanning calorimetric study. Biophys. Chem. 110 (2004) 119-128
16. Bobkov A.A., Muhlrad A., Pavlov D.A., Kokabi K., Yilmaz A., and Reisler E. Cooperative effects of cofilin (ADF) on actin structure suggest allosteric mechanism of cofilin function. J. Mol. Biol. 356 (2006) 325-334
17. Kudryashov D.S., Sawaya M.R., Adisetiyo H., Norcross T., Hegyi G., Reisler E., and Yeates T.O. The crystal structure of a cross-linked actin dimer suggests a detailed molecular interface in F-actin. Proc. Natl Acad. Sci. USA 102 (2005) 13105-13110
18. Prochniewicz E., Janson N., Thomas D.D., and De La Cruz E.M. Cofilin increases the torsional flexibility and dynamics of actin filaments. J. Mol. Biol. 353 (2005) 990-1000
19. Galkin V.E., Orlova A., VanLoock M.S., Shvetsov A., Reisler E., and Egelman E.H. ADF/cofilin use an intrinsic mode of F-actin instability to disrupt actin filaments. J. Cell Biol. 163 (2003) 1057-1066
20. Galkin V.E., VanLoock M.S., Orlova A., and Egelman E.H. A new internal mode in F-actin helps explain the remarkable evolutionary conservation of actin's sequence and structure. Curr. Biol. (Cambridge) 12 (2002) 570-575
21. McGough A., Chiu W., and Way M. Determination of the gelsolin binding site on F-actin: implications for severing and capping. Biophys. J. 74 (1998) 764-772
22. Orlova A., Prochniewicz E., and Egelman E.H. Structural dynamics of F-actin. II. Cooperativity in structural transitions. J. Mol. Biol. 245 (1995) 598-607
23. McGough A.M., Staiger C.J., Min J.K., and Simonetti K.D. The gelsolin family of actin regulatory proteins: modular structures, versatile functions. FEBS Letters 552 (2003) 75-81
24. Bamburg J.R., McGough A., and Ono S. Putting a new twist on actin: ADF/cofilins modulate actin dynamics. Trends Cell Biol. 9 (1999) 364-370
25. Takashi R. A novel actin label: a fluorescent probe at glutamine-41 and its consequences. Biochemistry 27 (1988) 938-943
26. Kim E., Motoki M., Seguro K., Muhlrad A., and Reisler E. Conformational changes in subdomain 2 of G-actin: fluorescence probing by dansyl ethylenediamine attached to Gln-41. Biophys. J. 69 (1995) 2024-2032
27. Muhlrad A., Kudryashov D., Michael Peyser Y., Bobkov A.A., Almo S.C., and Reisler E. Cofilin induced conformational changes in F-actin expose subdomain 2 to proteolysis. J. Mol. Biol. 342 (2004) 1559-1567
28. Pavlov D., Muhlrad A., Cooper J., Wear M., and Reisler E. Severing of F-actin by yeast cofilin is pH-independent. Cell Motil. Cytoskel. 63 (2006) 533-542
29. Uyeda T.Q.P., Kron S.J., and Spudich J.A. Myosin step size: estimation from slow sliding movement of actin over low densities of heavy meromyosin. J. Mol. Biol. 214 (1990) 699-710
30. Wakabayashi T., Huxley H.E., Amos L.A., and Klug A. Three-dimensional image reconstruction of actin-tropomyosin complex and actin-tropomyosin-troponin-T-troponin I complex. J. Mol. Biol. 93 (1975) 477-497
31. Thomas D.D., Seidel J.C., and Gergely J. Rotational dynamics of spin-labeled F-actin in the sub-millisecond time range. J. Mol. Biol. 132 (1979) 257-273
32. Hegyi G., and Belagyi J. Intermonomer cross-linking of F-actin alters the dynamics of its interaction with H-meromyosin in the weak-binding state. FEBS J. 273 (2006) 1896-1905
33. Prochniewicz E., Walseth T.F., and Thomas D.D. Structural dynamics of actin during active interaction with myosin: different effects of weakly and strongly bound myosin heads. Biochemistry 43 (2004) 10642-10652
34. Burlacu S., and Borejdo J. Motion of actin-filaments in the presence of myosin heads and ATP. Biophys. J. 63 (1992) 1471-1482
35. Chan A.Y., Bailly M., Zebda N., Segall J.E., and Condeelis J.S. Role of cofilin in epidermal growth factor-stimulated actin polymerization and lamellipod protrusion. J. Cell Biol. 148 (2000) 531-542
36. Southwick F.S. Gelsolin and ADF/cofilin enhance the actin dynamics of motile cells. Proc. Natl Acad. Sci. USA 97 (2000) 6936-6938
37. De La Cruz E.M. Cofilin binding to muscle and non-muscle actin filaments: isoform-dependent cooperative interactions. J. Mol. Biol. 346 (2005) 557-564
38. McGough A., and Chiu W. ADF/cofilin weakens lateral contacts in the actin filament. J. Mol. Biol. 291 (1999) 513-519
39. Andrianantoandro E., and Pollard T.D. Mechanism of actin filament turnover by severing and nucleation at different concentrations of ADF/cofilin. Mol. Cell 24 (2006) 13-23
40. Miller C.J., Wong W.W., Bobkova E., Rubenstein P.A., and Reisler E. Mutational analysis of the role of the N terminus of actin in actomyosin interactions. Comparison with other mutant actins and implications for the cross-bridge cycle. Biochemistry 35 (1996) 16557-16565
41. Kurokawa H., Jujii W., Ohmi K., Sakurai T., and Nonomura Y. Simple and rapid purificiation of brevin. Biochem. Biophys. Res. Commun. 168 (1990) 451-457
42. Bobkov A.A., Muhlrad A., Kokabi K., Vorobiev S., Almo S.C., and Reisler E. Structural effects of cofilin on longitudinal contacts in F-actin. J. Mol. Biol. 323 (2002) 739-750
43. Palmgren S., Ojala P.J., Wear M.A., Cooper J.A., and Lappalainen P. Interactions with PIP2, ADP-actin monomers, and capping protein regulate the activity and localization of yeast twinfilin. J. Cell Biol. 155 (2001) 251-260
44. Umemoto S., and Sellers J.R. Characterization of in vitro motility assays using smooth muscle and cytoplasmic myosins. J. Biol. Chem. 265 (1990) 14864-14869