ArticleProtein science : a publication of the Protein Society2013
Electron paramagnetic resonance analysis of the vimentin tail domain reveals points of order in a largely disordered region and conformational adaptation upon filament assembly.
Article in Protein science : a publication of the Protein Society, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 33 citations in OpenAlex.
- Solid state NMR characterization of wild-type and mutant GFAP intermediate filament assemblies.bioRxiv : the preprint server for biology · 2026Article
- Metal Ion Binding of Vimentin Tail Domain Fragments.Chembiochem : a European journal of chemical biology · 2026Article
- Review
- Type III intermediate filaments in redox interplay: key role of the conserved cysteine residue.Biochemical Society transactions · 2024Review
- Article
- Adsorption of Diclofenac and PFBS on a Hair Keratin Dimer.The journal of physical chemistry. B · 2024Article
- Vimentin Tail Segments Are Differentially Exposed at Distinct Cellular Locations and in Response to Stress.Frontiers in cell and developmental biology · 2022Article
- Review
- Molecular Insight into the Regulation of Vimentin by Cysteine Modifications and Zinc Binding.Antioxidants (Basel, Switzerland) · 2021Article
- Addressing the Molecular Mechanism of Longitudinal Lamin Assembly Using Chimeric Fusions.Cells · 2020Article
- Electron Paramagnetic Resonance as a Tool for Studying Membrane Proteins.Biomolecules · 2020Review
- Completion of the Vimentin Rod Domain Structure Using Experimental Restraints: A New Tool for Exploring Intermediate Filament Assembly and Mutations.Structure (London, England : 1993) · 2019Article
- Vimentin filaments interact with the actin cortex in mitosis allowing normal cell division.Nature communications · 2019Article
- Production of recombinant human tektin 1, 2, and 4 and in vitro assembly of human tektin 1.Cytoskeleton (Hoboken, N.J.) · 2018Article
- Complete Structure of an Epithelial Keratin Dimer: Implications for Intermediate Filament Assembly.PloS one · 2015Article
- Use of electron paramagnetic resonance to solve biochemical problems.Biochemistry · 2013Review
- Antimitochondrial antibody recognition and structural integrity of the inner lipoyl domain of the E2 subunit of pyruvate dehydrogenase complex.Journal of immunology (Baltimore, Md. : 1950) · 2013Article
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Authors and funding
5 authors at 1 institution in 1 country.
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Abstract
Very little data have been reported that describe the structure of the tail domain of any cytoplasmic intermediate filament (IF) protein. We report here the results of studies using site directed spin labeling and electron paramagnetic resonance (SDSL-EPR) to explore the structure and dynamics of the tail domain of human vimentin in tetramers (protofilaments) and filaments. The data demonstrate that in contrast to the vimentin head and rod domains, the tail domains are not closely apposed in protofilaments. However, upon assembly into intact IFs, several sites, including positions 445, 446, 451, and 452, the conserved "beta-site," become closely apposed, indicating dynamic changes in tail domain structure that accompany filament elongation. No evidence is seen for coiled-coil structure within the region studied, in either protofilaments or assembled filaments. EPR analysis also establishes that more than half of the tail domain is very flexible in both the assembly intermediate and the intact IF. However, by positioning the spin label at distinct sites, EPR is able to identify both the rod proximal region and sites flanking the beta-site motif as rigid locations within the tail. The rod proximal region is well assembled at the tetramer stage with only slight changes occurring during filament elongation. In contrast, at the beta site, the polypeptide backbone transitions from flexible in the assembly intermediate to much more rigid in the intact IF. These data support a model in which the distal tail domain structure undergoes significant conformational change during filament elongation and final assembly.
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