Journal
NANOSCALE
Volume 12, Issue 28, Pages 15236-15245Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/d0nr02778b
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Funding
- European Research Council (ERC) under the European Union's Horizon 2020 Research and Innovation Program [724932]
- German Federal Ministry of Education and Research (BMBF)
- Max Planck Society
- Excellence Fellowship of the International Max Planck Research School for Physics of Biological and Complex Systems (IMPRS PBCS)
- Studienstiftung des deutschen Volkes e.V.
- European Research Council (ERC) [724932] Funding Source: European Research Council (ERC)
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The cytoskeleton is formed by three types of filamentous proteins - microtubules, actin filaments, and intermediate filaments (IFs) - and enables cells to withstand external and internal forces. Vimentin is the most abundant IF protein in humans and assembles into 10 nm diameter filaments with remarkable mechanical properties, such as high extensibility and stability. It is, however, unclear to which extent these properties are influenced by the electrostatic environment. Here, we study the mechanical properties of single vimentin filaments by employing optical trapping combined with microfluidics. Force-strain curves, recorded at varying ion concentrations and pH values, reveal that the mechanical properties of single vimentin IFs are influenced by pH and ion concentration. By combination with Monte Carlo simulations, we relate these altered mechanics to electrostatic interactions of subunits within the filaments. We thus suggest possible mechanisms that allow cells to locally tune their stiffness without remodeling the entire cytoskeleton.
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