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Human cofilin forms oligomers exhibiting actin bundling activity

MPG-Autoren
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Pfannstiel,  Jörg
Emeritus Group Bioorganic Chemistry, Max Planck Institute for Medical Research, Max Planck Society;

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Shoeman,  Robert L.
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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Faulstich,  Heinz
Department of Molecular Cell Research, Max Planck Institute for Medical Research, Max Planck Society;

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Zitation

Pfannstiel, J., Cyrklaff, M., Habermann, A., Stoeva, S., Griffiths, G., Shoeman, R. L., et al. (2001). Human cofilin forms oligomers exhibiting actin bundling activity. The Journal of Biological Chemistry, 276(52), 49476-49484. doi:10.1074/jbc.M104760200.


Zitierlink: http://hdl.handle.net/11858/00-001M-0000-0028-FE85-D
Zusammenfassung
Human cofilin possesses the tendency for self-association, as indicated by the rapid formation of dimers and oligomers when reacted with water-soluble carbodiimide, Ellman's reagent, or glutathione disulfide. Intermolecular disulfide bonds involve Cys(39) and probably Cys(147) of two adjacent cofilin units. The disulfide-linked dimers and oligomers exhibit a biological activity distinct from the monomer. While monomeric cofilin decreased viscosity and light-scattering of F-actin solutions, dimers and oligomers caused an increase in viscosity and light scattering. Electron microscopy revealed that cofilin oligomers induce the formation of highly ordered actin bundles with occasionally blunt ends similar to actin-cofilin rods observed in cells under oxidative stress. Bundling activity of the disulfide-linked oligomers could be completely reversed into severing activity by dithiothreitol. Formation of cofilin oligomers occurred also in the presence of actin at pH 8, but not at pH 6.6, and was significantly enhanced in the presence of phosphatidylinositol 4,5-bisphosphate. Our data are consistent with the idea that cofilin exists in two forms in vivo also: as monomers exhibiting the known severing activity and as oligomers exhibiting actin bundling activity. However, stabilization of cofilin oligomers in cytoplasm is probably achieved not by disulfide bonds but by a local increase in cofilin concentration and/or binding of regulatory proteins.