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  The Small Heat Shock Protein Hsp27 Affects Assembly Dynamics and Structure of Keratin Intermediate Filament Networks

Kayser, J., Haslbeck, M., Dempfle, L., Krause, M., Grashoff, C., Buchner, J., et al. (2013). The Small Heat Shock Protein Hsp27 Affects Assembly Dynamics and Structure of Keratin Intermediate Filament Networks. BIOPHYSICAL JOURNAL, 105(8), 1778-1785. doi:10.1016/j.bpj.2013.09.007.

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Item Permalink: https://hdl.handle.net/21.11116/0000-000F-2E68-A Version Permalink: https://hdl.handle.net/21.11116/0000-000F-2EB3-4
Genre: Journal Article

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Articles published under an Elsevier user license are protected by copyright and may be used for non-commercial purposes. Users may access, download, copy, translate, text mine and data mine the articles.
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 Creators:
Kayser, Jona1, Author
Haslbeck, Martin2, Author
Dempfle, Lisa2, Author
Krause, Maike2, Author
Grashoff, Carsten2, Author
Buchner, Johannes2, Author
Herrmann, Harald2, Author
Bausch, Andreas R.2, Author
Affiliations:
1External Organizations, ou_persistent22              
2external, ou_persistent22              

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 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.

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Language(s): eng - English
 Dates: 2013-10-15
 Publication Status: Issued
 Pages: -
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 Table of Contents: -
 Rev. Type: -
 Identifiers: ISI: 000325838500007
DOI: 10.1016/j.bpj.2013.09.007
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Title: BIOPHYSICAL JOURNAL
Source Genre: Journal
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Pages: - Volume / Issue: 105 (8) Sequence Number: - Start / End Page: 1778 - 1785 Identifier: ISSN: 0006-3495