ArticleBiophysical journal2014
Direct observation of subunit exchange along mature vimentin intermediate filaments.
Article in Biophysical journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
37 citing papers in PubMed, 70 citations in OpenAlex.
- Keratin filaments and soluble vimentin interact with isoform specificity to organize cell signaling.Genes & development · 2026Article
- Segmental Mechanobiology of Normal and Glaucomatous Human Trabecular Meshwork Cells.ACS measurement science au · 2026Article
- Insights into the Structure of Intermediate Filaments.Sub-cellular biochemistry · 2026Review
- Intermediate Filaments: Structure-Mechanics Crosstalk.Sub-cellular biochemistry · 2026Review
- Continuous self-repair protects vimentin intermediate filaments from fragmentation.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Article
- How cytoskeletal crosstalk makes cells move: Bridging cell-free and cell studies.Biophysics reviews · 2024Review
- Vimentin filaments integrate low-complexity domains in a complex helical structure.Nature structural & molecular biology · 2024Article
- Intermediate, but not average: The unusual lives of the nuclear lamin proteins.Current opinion in cell biology · 2023Review
- Genetic Insights into Primary Restrictive Cardiomyopathy.Journal of clinical medicine · 2022Review
- A general mathematical model for the in vitro assembly dynamics of intermediate filament proteins.Biophysical journal · 2022Article
- Molecular organization and mechanics of single vimentin filaments revealed by super-resolution imaging.Science advances · 2022Article
- Impact of Vimentin on Regulation of Cell Signaling and Matrix Remodeling.Frontiers in cell and developmental biology · 2022Review
- Intermediate Filaments in Cellular Mechanoresponsiveness: Mediating Cytoskeletal Crosstalk From Membrane to Nucleus and Back.Frontiers in cell and developmental biology · 2022Review
- ALD-R491 regulates vimentin filament stability and solubility, cell contractile force, cell migration speed and directionality.Frontiers in cell and developmental biology · 2022Article
- Review
- The vimentin cytoskeleton: when polymer physics meets cell biology.Physical biology · 2020Article
- Vimentin S-glutathionylation at Cys328 inhibits filament elongation and induces severing of mature filaments in vitro.The FEBS journal · 2020Article
- 14-3-3 targets keratin intermediate filaments to mechanically sensitive cell-cell contacts.Molecular biology of the cell · 2020Article
- Vimentin disruption by lipoxidation and electrophiles: Role of the cysteine residue and filament dynamics.Redox biology · 2019Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Actin filaments, microtubules, and intermediate filaments (IFs) are central elements of the metazoan cytoskeleton. At the molecular level, the assembly mechanism for actin filaments and microtubules is fundamentally different from that of IFs. The former two types of filaments assemble from globular proteins. By contrast, IFs assemble from tetrameric complexes of extended, half-staggered, and antiparallel oriented coiled-coils. These tetramers laterally associate into unit-length filaments; subsequent longitudinal annealing of unit-length filaments yields mature IFs. In vitro, IFs form open structures without a fixed number of tetramers per cross-section along the filament. Therefore, a central question for the structural biology of IFs is whether individual subunits can dissociate from assembled filaments and rebind at other sites. Using the fluorescently labeled IF-protein vimentin for assembly, we directly observe and quantitatively determine subunit exchange events between filaments as well as with soluble vimentin pools. Thereby we demonstrate that the cross-sectional polymorphism of donor and acceptor filaments plays an important role. We propose that in segments of donor filaments with more than the standard 32 molecules per cross-section, subunits are not as tightly bound and are predisposed to be released from the filament.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.