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Analogous F-actin binding by cofilin and gelsolin segment 2 substantiates their structural relationship

Marleen Van Troys (UGent) , Daisy Dewitte, Jean-Luc Verschelde, Mark Goethals, Joël Vandekerckhove (UGent) and Christophe Ampe (UGent)
(1997) JOURNAL OF BIOLOGICAL CHEMISTRY. 272(52). p.32750-32758
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Abstract
Cofilin is representative for a family of low molecular weight actin filament binding and depolymerizing proteins. Recently the three-dimensional structure of yeast cofilin and of the cofilin homologs destrin and actophorin were resolved, and a striking similarity to segments of gelsolin and related proteins was observed (Hatanaka, H., Ogura, K., Moriyama, K., Ichikawa, S., Yahara, I., and Inagaka, F. (1996) Cell 85, 1047-1055; Fedorov, A. A., Lappalainen, P., Fedorov, E. V., Drubin, D. G., and Almo, S. C. (1997) Not. Struct. Biol. 4, 366-369; Leonard, S. A., Gittis, A. G., Petrella, E. C., Pollard, T. D., and Lattman, E. E. (1997) Not. Struct. Biol. 4, 369-373). Using peptide mimetics, we show that the actin binding site stretches over the entire cofilin alpha-helix 112-128. In addition, we demonstrate that cofilin and its actin binding peptide compete with gelsolin segments 2-3 for binding to actin filaments. Based on these competition data, we propose that cofilin and segment 2 of gelsolin use a common structural topology to bind to actin and probably share a similar target site on the filament. This adds a functional dimension to their reported structural homology, and this F-actin binding mode provides a basis to further enlighten the effect of members of the cofilin family on actin filament dynamics.
Keywords
PORCINE BRAIN, DEPOLYMERIZING FACTOR, MUTATIONAL ANALYSIS, ALPHA-ACTININ, PROTEIN, SITE, IDENTIFICATION, FILAMENTS, POLYMERIZATION, SEQUENCE

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Citation

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MLA
Van Troys, Marleen, Daisy Dewitte, Jean-Luc Verschelde, et al. “Analogous F-actin Binding by Cofilin and Gelsolin Segment 2 Substantiates Their Structural Relationship.” JOURNAL OF BIOLOGICAL CHEMISTRY 272.52 (1997): 32750–32758. Print.
APA
Van Troys, M., Dewitte, D., Verschelde, J.-L., Goethals, M., Vandekerckhove, J., & Ampe, C. (1997). Analogous F-actin binding by cofilin and gelsolin segment 2 substantiates their structural relationship. JOURNAL OF BIOLOGICAL CHEMISTRY, 272(52), 32750–32758.
Chicago author-date
Van Troys, Marleen, Daisy Dewitte, Jean-Luc Verschelde, Mark Goethals, Joël Vandekerckhove, and Christophe Ampe. 1997. “Analogous F-actin Binding by Cofilin and Gelsolin Segment 2 Substantiates Their Structural Relationship.” Journal of Biological Chemistry 272 (52): 32750–32758.
Chicago author-date (all authors)
Van Troys, Marleen, Daisy Dewitte, Jean-Luc Verschelde, Mark Goethals, Joël Vandekerckhove, and Christophe Ampe. 1997. “Analogous F-actin Binding by Cofilin and Gelsolin Segment 2 Substantiates Their Structural Relationship.” Journal of Biological Chemistry 272 (52): 32750–32758.
Vancouver
1.
Van Troys M, Dewitte D, Verschelde J-L, Goethals M, Vandekerckhove J, Ampe C. Analogous F-actin binding by cofilin and gelsolin segment 2 substantiates their structural relationship. JOURNAL OF BIOLOGICAL CHEMISTRY. 1997;272(52):32750–8.
IEEE
[1]
M. Van Troys, D. Dewitte, J.-L. Verschelde, M. Goethals, J. Vandekerckhove, and C. Ampe, “Analogous F-actin binding by cofilin and gelsolin segment 2 substantiates their structural relationship,” JOURNAL OF BIOLOGICAL CHEMISTRY, vol. 272, no. 52, pp. 32750–32758, 1997.
@article{176004,
  abstract     = {Cofilin is representative for a family of low molecular weight actin filament binding and depolymerizing proteins. Recently the three-dimensional structure of yeast cofilin and of the cofilin homologs destrin and actophorin were resolved, and a striking similarity to segments of gelsolin and related proteins was observed (Hatanaka, H., Ogura, K., Moriyama, K., Ichikawa, S., Yahara, I., and Inagaka, F. (1996) Cell 85, 1047-1055; Fedorov, A. A., Lappalainen, P., Fedorov, E. V., Drubin, D. G., and Almo, S. C. (1997) Not. Struct. Biol. 4, 366-369; Leonard, S. A., Gittis, A. G., Petrella, E. C., Pollard, T. D., and Lattman, E. E. (1997) Not. Struct. Biol. 4, 369-373). Using peptide mimetics, we show that the actin binding site stretches over the entire cofilin alpha-helix 112-128. In addition, we demonstrate that cofilin and its actin binding peptide compete with gelsolin segments 2-3 for binding to actin filaments. Based on these competition data, we propose that cofilin and segment 2 of gelsolin use a common structural topology to bind to actin and probably share a similar target site on the filament. This adds a functional dimension to their reported structural homology, and this F-actin binding mode provides a basis to further enlighten the effect of members of the cofilin family on actin filament dynamics.},
  author       = {Van Troys, Marleen and Dewitte, Daisy and Verschelde, Jean-Luc and Goethals, Mark and Vandekerckhove, Joël and Ampe, Christophe},
  issn         = {0021-9258},
  journal      = {JOURNAL OF BIOLOGICAL CHEMISTRY},
  keywords     = {PORCINE BRAIN,DEPOLYMERIZING FACTOR,MUTATIONAL ANALYSIS,ALPHA-ACTININ,PROTEIN,SITE,IDENTIFICATION,FILAMENTS,POLYMERIZATION,SEQUENCE},
  language     = {eng},
  number       = {52},
  pages        = {32750--32758},
  title        = {Analogous F-actin binding by cofilin and gelsolin segment 2 substantiates their structural relationship},
  url          = {http://dx.doi.org/10.1074/jbc.272.52.32750},
  volume       = {272},
  year         = {1997},
}
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