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Vimentin filaments integrate low complexity domains in a highly complex helical structure
Open accessPreprint — published as 10.1038/s41594-024-01261-2 · Paper page
Abstract
Intermediate filaments (IFs) are integral components of the cytoskeleton. They provide cells with tissue-specific mechanical properties and are involved in numerous cellular processes. Due to their intricate architecture, a 3D structure of IFs has remained elusive. Here we use cryo-focused ion beam milling, cryo-electron microscopy and tomography, to obtain a 3D structure of vimentin IFs (VIFs). VIFs assemble into a modular, densely-packed and highly-ordered helical symmetric structure of 40 α-helices in cross-section, organized into 5 protofibrils. Surprisingly, the intrinsically disordered head domains form an amyloid-like fiber in the center of VIFs, while the intrinsically disordered tails form lateral connections between the protofibrils. Our findings demonstrate how protein domains of low sequence complexity can complement well-folded protein domains to construct a biopolymer with striking strength and stretchability.
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Metadata
- Authors
- Eibauer, M., Weber, M. S., Kronenberg-Tenga, R., Beales, C. T., Boujemaa-Paterski, R., Turgay, Y., Sivagurunathan, S., Kraxner, J., Köster, S., Goldman, R. D., & Medalia, O.
- Affiliations
- University of Zurich (CH)
- Northwestern University (US)
- Max Delbrück Center (DE)
- University of Göttingen (DE)
- Corresponding author
- Eibauer, Matthias
- Medalia, Ohad
- ORCID
- Venue
- Nature Structural & Molecular Biology
- Publisher
- openRxiv
- Published
- 2023-05-22
- Volume
- 31
- Issue
- 6
- Pages
- 939-949
- ISSN
- 1545-9985 (ISSN-L)
- PMC
- PMC11189308
- OpenAlex
- W4394881895
- Cited by
- 87
- References
- 1
- Citations by year
- 2026: 27 · 2025: 34 · 2024: 17 · 2023: 9
- FWCI
- 17.45
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- cc-by
- Locations
- Nature Structural & Molecular Biology (publishedVersion, cc-by)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- GoeScholar The Publication Server of the Georg-August-Universität Göttingen (Georg-August-Universität Göttingen) (submittedVersion, cc-by)
- Zurich Open Repository and Archive (University of Zurich) (submittedVersion, cc-by)
- Funders
- National Science Foundation
- Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung (207453)
- Universität Zürich
- Åbo Akademi
- Mäxi-Stiftung
- National Institutes of Health
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Skin and Cellular Biology Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular Mechanics and Interactions
- Keywords
- vimentin, intermediate filaments, intrinsically disordered regions, low-complexity domains, cytoskeleton mechanics
- MeSH terms
- Protein Domains, Protein Conformation, alpha-Helical, Humans, Intermediate Filaments, Models, Molecular, Vimentin, Cryoelectron Microscopy
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