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  Post-translational modifications soften vimentin intermediate filaments

Kraxner, J., Lorenz, C., Menzel, J., Parfentev, I., Silbern, I., Denz, M., et al. (2021). Post-translational modifications soften vimentin intermediate filaments. Nanoscale, 13(1), 380-387. doi:10.1039/D0NR07322A.

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Kraxner, J., Author
Lorenz, C., Author
Menzel, J., Author
Parfentev, I.1, Author           
Silbern, I.1, Author           
Denz, M., Author
Urlaub, H.1, Author           
Schwappach, B., Author
Köster, S., Author
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1Research Group of Bioanalytical Mass Spectrometry, MPI for Biophysical Chemistry, Max Planck Society, ou_578613              

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 Abstract: The mechanical properties of biological cells are determined by the cytoskeleton, a composite biopolymer network consisting of microtubules, actin filaments and intermediate filaments (IFs). By differential expression of cytoskeletal proteins, modulation of the network architecture and interactions between the filaments, cell mechanics may be adapted to varying requirements on the cell. Here, we focus on the intermediate filament protein vimentin and introduce post-translational modifications as an additional, much faster mechanism for mechanical modulation. We study the impact of phosphorylation on filament mechanics by recording force-strain curves using optical traps. Partial phosphorylation softens the filaments. We show that binding of the protein 14-3-3 to phosphorylated vimentin IFs further enhances this effect and speculate that in the cell 14-3-3 may serve to preserve the softening and thereby the altered cell mechanics. We explain our observation by the additional charges introduced during phosphorylation.

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Language(s): eng - English
 Dates: 2020-12-102021-01-07
 Publication Status: Issued
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 Rev. Type: Peer
 Identifiers: DOI: 10.1039/D0NR07322A
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Title: Nanoscale
Source Genre: Journal
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Pages: - Volume / Issue: 13 (1) Sequence Number: - Start / End Page: 380 - 387 Identifier: ISSN: 2040-3364
ISSN: 2040-3372