8rve

Publication Abstract from PubMed

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 alpha-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.

Vimentin filaments integrate low-complexity domains in a complex helical structure.,Eibauer M, Weber MS, Kronenberg-Tenga R, Beales CT, Boujemaa-Paterski R, Turgay Y, Sivagurunathan S, Kraxner J, Koster S, Goldman RD, Medalia O Nat Struct Mol Biol. 2024 Jun;31(6):939-949. doi: 10.1038/s41594-024-01261-2. , Epub 2024 Apr 17. PMID:38632361^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.