Ion type and valency differentially drive vimentin tetramers into intermediate filaments or higher order assemblies

Denz, Manuela; Marschall, Manuel; Herrmann, Harald; Köster, Sarah

doi:10.1039/d0sm01659d

Cited by 14 publications

(26 citation statements)

References 42 publications

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“…To investigate the cause of the network stiffening, we analyze the temporal evolution of the filament length. Vimentin filament assembly strongly depends on the ionic strength of the utilized buffer (13)(14)(15)(16), and the type and concentration of the ions influence the filament structure (13,(17)(18)(19)(20)(21). Specifically, the formation kinetics, architecture, and mechanics of the networks depend on a careful balance between the slow longitudinal assembly of single filaments and the lateral association of filaments-i.e., bundling.…”

Section: Significancementioning

confidence: 99%

Multiscale mechanics and temporal evolution of vimentin intermediate filament networks

Schepers

Lorenz

Nietmann

et al. 2021

Proc. Natl. Acad. Sci. U.S.A.

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The cytoskeleton, an intricate network of protein filaments, motor proteins, and cross-linkers, largely determines the mechanical properties of cells. Among the three filamentous components, F-actin, microtubules, and intermediate filaments (IFs), the IF network is by far the most extensible and resilient to stress. We present a multiscale approach to disentangle the three main contributions to vimentin IF network mechanics—single-filament mechanics, filament length, and interactions between filaments—including their temporal evolution. Combining particle tracking, quadruple optical trapping, and computational modeling, we derive quantitative information on the strength and kinetics of filament interactions. Specifically, we find that hydrophobic contributions to network mechanics enter mostly via filament-elongation kinetics, whereas electrostatics have a direct influence on filament–filament interactions.

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Section: Significancementioning

confidence: 99%

Multiscale mechanics and temporal evolution of vimentin intermediate filament networks

Schepers

Lorenz

Nietmann

et al. 2021

Proc. Natl. Acad. Sci. U.S.A.

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“…Already small changes in the amino acid sequence lead to completely different stretching behaviors for these filaments. But also the mechanical and structural properties for one type of IF can be individually tuned by the presence of different ions or variation of the pH [52,53]. The change of mechanics can be explained by electrostatic interactions of subunits within the filament.…”

Section: Variation Of Mechanical Properties Of Intermediate Filamentsmentioning

confidence: 99%

Vimentin Intermediate Filament Softening - Recovery Behavior and Post-Translational Modifications

Kraxner¹

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Matter to Life" Contribution to this article: S.K. conceived and supervised the project. J.K. performed the experiments and analyzed the data. J.M. and B.S. provided the 14-3-3 protein. H.U., I. P. and I. S. performed the mass spectrometry measurements. C.L. performed the numerical simulations. M.D. performed the small-angle X-ray scattering experiments. J.K. and S.K. wrote the manuscript with contributions from all authors.

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“…ULFs anneal longitudinal to an extended filament (sketches not to scale). Figure with minor adaptations from [22] under the Creative Commons Attribution (CC BY) license.…”

Section: Architecture and Assembly Of Intermediate Filamentsmentioning

confidence: 99%

“…It is important to note that throughout the assembly process the vimentin tetramer configurations are dynamic [18,23]. Despite the hierarchical assembly for vimentin ULFs, tetramer numbers per ULF are influenced by the surrounding ion type and ion concentration [22,24,25]. For vimentin, on average, 32 monomers are Architecture and Assembly of Intermediate Filaments 2.1 present in one ULF.…”

Section: Architecture and Assembly Of Intermediate Filamentsmentioning

confidence: 99%

“…For vimentin, on average, 32 monomers are Architecture and Assembly of Intermediate Filaments 2.1 present in one ULF. However, depending on the ionic strength during assembly, the number of monomers can increase by over 400 % per ULF [22]. Furthermore, the assembled filament remains a dynamical structure, as subunit exchanges of monomers in assembled filaments occur and mechanics are dependent on pH and ion charges [26,27].…”

Section: Architecture and Assembly Of Intermediate Filamentsmentioning

confidence: 99%

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Studying the Dynamics and Inhibition of Vimentin Assembly by Small-Angle X-ray Scattering

Brehm¹

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The combination of microfluidics and X-ray methods attracts a lot of attention from researchers as it brings together the high controllability of microfluidic sample environments and the small length scales probed by X-rays. In particular, the fields of biophysics and biology have benefited enormously from such approaches. We introduce a straightforward fabrication method for X-ray compatible microfluidic devices made solely from cyclic olefin copolymers. We benchmark the performance of the devices against other devices including more commonly used Kapton windows and obtain data of equal quality using small angle X-ray scattering. An advantage of the devices presented here is that no gluing between interfaces is necessary, rendering the production very reliable. As a biophysical application, we investigate the early time points of the assembly of vimentin intermediate filament proteins into higher-order structures. This weakly scattering protein system leads to high quality data in the new devices, thus opening up the way for numerous future applications.

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Ion type and valency differentially drive vimentin tetramers into intermediate filaments or higher order assemblies

Abstract: Our systematic study shows that vimentin forms individual 10 nm diameter filaments in the presence of monovalent ions and thicker filaments that aggregate into dense networks in the presence of multivalent ions.

Cited by 14 publications

References 42 publications

Multiscale mechanics and temporal evolution of vimentin intermediate filament networks

Multiscale mechanics and temporal evolution of vimentin intermediate filament networks

Vimentin Intermediate Filament Softening - Recovery Behavior and Post-Translational Modifications

Studying the Dynamics and Inhibition of Vimentin Assembly by Small-Angle X-ray Scattering

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