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| Title | Vimentin filaments integrate low-complexity domains in a complex helical structure. |
|---|---|
| Journal, issue, pages | Nat Struct Mol Biol, Year 2024 |
| Publish date | Apr 17, 2024 |
 Authors | Matthias Eibauer / Miriam S Weber / Rafael Kronenberg-Tenga / Charlie T Beales / Rajaa Boujemaa-Paterski / Yagmur Turgay / Suganya Sivagurunathan / Julia Kraxner / Sarah Köster / Robert D Goldman / Ohad Medalia /    |
| PubMed 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 ...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, intertwined and flexible helical structure of 40 α-helices in cross-section, organized into five protofibrils. Surprisingly, the intrinsically disordered head domains form a fiber in the lumen 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 mechanical strength and stretchability. |
 External links | Nat Struct Mol Biol / PubMed:38632361 |
| Methods | EM (helical sym.) / EM (subtomogram averaging) |
| Resolution | 7.2 - 20.2 Å |
| Structure data | EMDB-16844: Vimentin intermediate filament structure  EMDB-19562: Vimentin intermediate filament protofibril stoichiometry  EMDB-19563: Vimentin intermediate filament structure (delta tail) |
| Source |
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 Keywords |  STRUCTURAL PROTEIN / vimentin / intermediate filament / cytoskeleton |
