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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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 Creators:
Kayser, Jona1, Author
Haslbeck, Martin1, Author
Dempfle, Lisa1, Author
Krause, Maike1, Author
Grashoff, Carsten2, Author           
Buchner, Johannes1, Author
Herrmann, Harald1, Author
Bausch, Andreas R.1, Author
Affiliations:
1external, ou_persistent22              
2Grashoff, Carsten / Molecular Mechanotransduction, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565150              

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Free keywords: ALPHA-B-CRYSTALLIN; F-ACTIN NETWORKS; KINETICS DETERMINE; CELL; ARCHITECTURE; STRESS; ORGANIZATION; CYTOSKELETON; METASTASIS; MIGRATION
 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
 Publication Status: Issued
 Pages: 8
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: ISI: 000325838500007
DOI: 10.1016/j.bpj.2013.09.007
 Degree: -

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Title: BIOPHYSICAL JOURNAL
Source Genre: Journal
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Publ. Info: 600 TECHNOLOGY SQUARE, 5TH FLOOR, CAMBRIDGE, MA 02139 USA : CELL PRESS
Pages: - Volume / Issue: 105 (8) Sequence Number: - Start / End Page: 1778 - 1785 Identifier: ISSN: 0006-3495