
Analogous F-actin binding by cofilin and gelsolin segment 2 substantiates their structural relationship
- Author
- Marleen Van Troys (UGent) , Daisy Dewitte, Jean-Luc Verschelde, Mark Goethals, Joël Vandekerckhove (UGent) and Christophe Ampe (UGent)
- Organization
- 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
Please use this url to cite or link to this publication: http://hdl.handle.net/1854/LU-176004
- Chicago
- 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.
- 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.
- 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.
- 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.
@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, Jo{\"e}l and Ampe, Christophe}, issn = {0021-9258}, journal = {JOURNAL OF BIOLOGICAL CHEMISTRY}, 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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