ArticleProceedings of the National Academy of Sciences of the United States of America2006
Monitoring intermediate filament assembly by small-angle x-ray scattering reveals the molecular architecture of assembly intermediates.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.
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51 citing papers in PubMed, 119 citations in OpenAlex.
- Unraveling the molecular mechanisms of vimentin interaction with G-quadruplex repeats.Nucleic acids research · 2026Article
- The important interplay between metal ions and the intermediate filament protein vimentin.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2025Review
- Extracellular filaments revealed by affinity capture cryogenic-electron tomography.Nature communications · 2025Article
- Continuous self-repair protects vimentin intermediate filaments from fragmentation.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Hypersensitivity of the vimentin cytoskeleton to net-charge states and Coulomb repulsion.bioRxiv : the preprint server for biology · 2024Article
- Deciphering vimentin assembly: Bridging theoretical models and experimental approaches.Molecules and cells · 2024Review
- Vimentin filaments integrate low-complexity domains in a complex helical structure.Nature structural & molecular biology · 2024Article
- Characters of KRT80 and its roles in neoplasms diseases.Cancer medicine · 2023Review
- Molecular structure of soluble vimentin tetramers.Scientific reports · 2023Article
- Golgi-protein 73 facilitates vimentin polymerization in hepatocellular carcinoma.International journal of biological sciences · 2023Article
- Role of the Intermediate Filament Protein Peripherin in Health and Disease.International journal of molecular sciences · 2022Review
- Review
- Molecular Insight into the Regulation of Vimentin by Cysteine Modifications and Zinc Binding.Antioxidants (Basel, Switzerland) · 2021Article
- A proposed atomic model of the head-to-tail interaction in the filament structure of vimentin.Journal of biomolecular structure & dynamics · 2020Article
- Vimentin as a Multifaceted Player and Potential Therapeutic Target in Viral Infections.International journal of molecular sciences · 2020Review
- Zinc Differentially Modulates the Assembly of Soluble and Polymerized Vimentin.International journal of molecular sciences · 2020Article
- The Interface between Keratin Structurotype and Human Disease.Structure (London, England : 1993) · 2020Article
- Structure-Function Analyses of a Keratin Heterotypic Complex Identify Specific Keratin Regions Involved in Intermediate Filament Assembly.Structure (London, England : 1993) · 2020Article
- 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 disruption by lipoxidation and electrophiles: Role of the cysteine residue and filament dynamics.Redox biology · 2019Article
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Authors and funding
8 authors at 4 institutions in 5 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Intermediate filaments (IFs), along with microtubules, microfilaments, and associated cross-bridging proteins, constitute the cytoskeleton of metazoan cells. While crystallographic data on the dimer representing the elementary IF "building block" have recently become available, little structural detail is known about both the mature IF architecture and its assembly pathway. Here, we have applied solution small-angle x-ray scattering to investigate the in vitro assembly of a 53-kDa human IF protein vimentin at pH 8.4 by systematically varying the ionic strength conditions, and complemented these experiments by electron microscopy and analytical ultracentrifugation. While a vimentin solution in 5 mM Tris.HCl (pH 8.4) contains predominantly tetramers, addition of 20 mM NaCl induces further lateral assembly evidenced by the shift of the sedimentation coefficient and yields a distinct octameric intermediate. Four octamers eventually associate into unit-length filaments (ULFs) that anneal longitudinally. Based on the small-angle x-ray scattering experiments supplemented by crystallographic data and additional structural constraints, 3D molecular models of the vimentin tetramer, octamer, and ULF were constructed. Within each of the three oligomers, the adjacent dimers are aligned exclusively in an approximately half-staggered antiparallel A(11) mode with a distance of 3.2-3.4 nm between their axes. The ULF appears to be a dynamic and a relatively loosely packed structure with a roughly even mass distribution over its cross-section.
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