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

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Schlagwörter: ALPHA-B-CRYSTALLIN; F-ACTIN NETWORKS; KINETICS DETERMINE; CELL; ARCHITECTURE; STRESS; ORGANIZATION; CYTOSKELETON; METASTASIS; MIGRATION
 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.

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Sprache(n): eng - English
 Datum: 2013
 Publikationsstatus: Erschienen
 Seiten: 8
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: ISI: 000325838500007
DOI: 10.1016/j.bpj.2013.09.007
 Art des Abschluß: -

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Titel: BIOPHYSICAL JOURNAL
Genre der Quelle: Zeitschrift
 Urheber:
Affiliations:
Ort, Verlag, Ausgabe: 600 TECHNOLOGY SQUARE, 5TH FLOOR, CAMBRIDGE, MA 02139 USA : CELL PRESS
Seiten: - Band / Heft: 105 (8) Artikelnummer: - Start- / Endseite: 1778 - 1785 Identifikator: ISSN: 0006-3495