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Intermediate filaments are cytoskeletal proteins with higher tensile strength and flexibility than microfilaments and microtubules. Unlike the other two cytoskeletal proteins, intermediate filament formation lacks the enzymatic activity to hydrolyze nucleotides like ATP and GTP to generate energy for polymerization. Therefore, the formation of intermediate filaments is multistep self-assembly. The involvement of any accessory proteins in intermediate filament formation has not yet been...
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The intermediate filaments are an essential component of the cytoskeleton. Presently six types of intermediate filament have been identified. Type I and II are acidic and basic keratin proteins. Type III is of mesodermal origin and comprises four proteins: vimentin, desmin, glial fibrillary acidic protein (GFAP), and peripherin. Vimentin is commonly found in mesenchymal cells, desmin in muscle cells, GFAP in astrocytes, while peripherin is found in peripheral nervous system neurons (PNS). Type...
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The intermediate filaments are one of three widely studied cytoskeletal filaments. They are so named as their diameter (10 nm) is in between that of microfilaments (7 nm) and the microtubules (25 nm).  These filaments are highly stable and can remain intact when exposed to high salt concentrations and detergents. These filaments are responsible for providing stability and mechanical support to the cells. They also help in cell adhesion and maintaining tissue integrity.
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Post-translational modifications soften vimentin intermediate filaments.

Julia Kraxner1, Charlotta Lorenz, Julia Menzel

  • 1Institute for X-Ray Physics, University of Göttingen, 37077 Göttingen, Germany. sarah.koester@phys.uni-goettingen.de.

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Summary
This summary is machine-generated.

Post-translational modifications like phosphorylation rapidly alter intermediate filament mechanics. Phosphorylated vimentin softens, and 14-3-3 binding further enhances this softening, impacting cell mechanics.

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Area of Science:

  • Biophysics
  • Cell Biology
  • Biochemistry

Background:

  • Cellular mechanical properties are governed by the cytoskeleton, a complex network of biopolymers.
  • Intermediate filaments (IFs), including vimentin, are key components influencing cell mechanics.
  • Post-translational modifications offer a rapid mechanism for modulating filament properties.

Purpose of the Study:

  • To investigate the impact of vimentin phosphorylation on filament mechanics.
  • To explore the role of the 14-3-3 protein in modulating the mechanical properties of phosphorylated vimentin.

Main Methods:

  • Utilized optical traps to record force-strain curves of vimentin filaments.
  • Analyzed the mechanical changes in vimentin upon phosphorylation.
  • Assessed the effect of 14-3-3 protein binding to phosphorylated vimentin.

Main Results:

  • Partial phosphorylation of vimentin filaments leads to a softening effect.
  • Binding of 14-3-3 protein to phosphorylated vimentin further amplifies this softening.
  • The observed softening is attributed to the introduction of additional charges via phosphorylation.

Conclusions:

  • Post-translational modifications, specifically phosphorylation, provide a rapid means to tune intermediate filament mechanics.
  • The 14-3-3 protein may play a role in maintaining altered cell mechanics by stabilizing the softened state of phosphorylated vimentin.
  • Understanding these mechanisms is crucial for comprehending cell adaptation and mechanical regulation.