The small heat shock protein Hsp27 affects assembly dynamics and structure of keratin intermediate filament networks

31Citations
Citations of this article
43Readers
Mendeley users who have this article in their library.

Abstract

The mechanical properties of living cells are essential for many processes. They are defined by the cytoskeleton, a composite network of protein fibers. Thus, the precise control of its architecture is of paramount importance. Our knowledge about the molecular and physical mechanisms defining the network structure remains scarce, especially for the intermediate filament cytoskeleton. Here, we investigate the effect of small heat shock proteins on the keratin 8/18 intermediate filament cytoskeleton using a well-controlled model system of reconstituted keratin networks. We demonstrate that Hsp27 severely alters the structure of such networks by changing their assembly dynamics. Furthermore, the C-terminal tail domain of keratin 8 is shown to be essential for this effect. Combining results from fluorescence and electron microscopy with data from analytical ultracentrifugation reveals the crucial role of kinetic trapping in keratin network formation. © 2013 Biophysical Society.

Cite

CITATION STYLE

APA

Kayser, J., Haslbeck, M., Dempfle, L., Krause, M., Grashoff, C., Buchner, J., … Bausch, A. R. (2013). The small heat shock protein Hsp27 affects assembly dynamics and structure of keratin intermediate filament networks. Biophysical Journal, 105(8), 1778–1785. https://doi.org/10.1016/j.bpj.2013.09.007

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free