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Schlagwörter:
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Zusammenfassung:
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.
