ArticleThe Journal of biological chemistry2010
Site-directed spin labeling and electron paramagnetic resonance determination of vimentin head domain structure.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed.
- 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
- Article
- Molecular structure of soluble vimentin tetramers.Scientific reports · 2023Article
- Impact of N-Terminal Tags on De Novo Vimentin Intermediate Filament Assembly.International journal of molecular sciences · 2022Article
- Unbiased peptoid cell screen identifies a peptoid targeting newly appeared cell surface vimentin on tumor transformed early lung cancer cells.Bioorganic & medicinal chemistry · 2022Article
- Vimentin Tail Segments Are Differentially Exposed at Distinct Cellular Locations and in Response to Stress.Frontiers in cell and developmental biology · 2022Article
- Review
- 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
- Investigation of the Hydration State of Self-Assembled Peptide Nanostructures with Advanced Electron Paramagnetic Resonance Spectroscopy.ACS omega · 2019Article
- Molecular insights into cardiomyopathies associated with desmin (DES) mutations.Biophysical reviews · 2018Review
- Phosphoproteome ofThe American journal of tropical medicine and hygiene · 2017Article
- Structural Dynamics of the Vimentin Coiled-coil Contact Regions Involved in Filament Assembly as Revealed by Hydrogen-Deuterium Exchange.The Journal of biological chemistry · 2016Article
- Proteomic Analysis Revealed the Important Role of Vimentin in Human Cervical Carcinoma HeLa Cells Treated With Gambogic Acid.Molecular & cellular proteomics : MCP · 2016Article
- 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
- Electron paramagnetic resonance analysis of the vimentin tail domain reveals points of order in a largely disordered region and conformational adaptation upon filament assembly.Protein science : a publication of the Protein Society · 2013Article
- The structure of vimentin linker 1 and rod 1B domains characterized by site-directed spin-labeling electron paramagnetic resonance (SDSL-EPR) and X-ray crystallography.The Journal of biological chemistry · 2012Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
Intermediate filament (IF) proteins have been predicted to have a conserved tripartite domain structure consisting of a largely alpha-helical central rod domain, flanked by head and tail domains. However, crystal structures have not been reported for any IF or IF protein. Although progress has been made in determining central rod domain structure, no structural data have been reported for either the head or tail domains. We used site-directed spin labeling and electron paramagnetic resonance to analyze 45 different spin labeled mutants spanning the head domain of vimentin. The data, combined with results from a previous study, provide strong evidence that the polypeptide backbones of the head domains form a symmetric dimer of closely apposed backbones that fold back onto the rod domain, imparting an asymmetry to the dimer. By following the behavior of spin labels during the process of in vitro assembly, we show that head domain structure is dynamic, changing as a result of filament assembly. Finally, because the vimentin head domain is the major site of the phosphorylation that induces disassembly at mitosis, we studied the effects of phosphorylation on head domain structure and demonstrate that phosphorylation drives specific head domain regions apart. These data provide the first evidence-based model of IF head domain structure.
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Registered trials
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.