ReviewCurrent opinion in cell biology2023
How do disordered head domains assist in the assembly of intermediate filaments?
Review in Current opinion in cell biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
12 citing papers in PubMed, 16 citations in OpenAlex.
- Solid state NMR characterization of wild-type and mutant GFAP intermediate filament assemblies.bioRxiv : the preprint server for biology · 2026Article
- Insights into the Structure of Intermediate Filaments.Sub-cellular biochemistry · 2026Review
- Vimentin intermediate filaments as structural and mechanical coordinators of mesenchymal cells.Nature cell biology · 2025Review
- [Advances in the Structure and Function of Neurofilament Protein and Its Application in Early Diagnosis of Amyotrophic Lateral Sclerosis].Sichuan da xue xue bao. Yi xue ban = Journal of Sichuan University. Medical science edition · 2025Review
- A simple method for mapping the location of cross-β-forming regions within protein domains of low sequence complexity.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Vimentin undergoes liquid-liquid phase separation to form droplets which wet and stabilize actin fibers.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Engineered Recombinant Hagfish Intermediate Filament Proteins: Unraveling Domain Roles in Synthetic Fiber Formation and Mechanics.ACS omega · 2024Article
- Oxidative stress elicits the remodeling of vimentin filaments into biomolecular condensates.Redox biology · 2024Article
- Review
- Neurofilament Biophysics: From Structure to Biomechanics.Molecular biology of the cell · 2024Review
- Protein domains of low sequence complexity-dark matter of the proteome.Genes & development · 2024Article
- Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 2 countries.
Funding
Abstract
The dominant structural feature of intermediate filament (IF) proteins is a centrally located α-helix. These long α-helical segments become paired in a parallel orientation to form coiled-coil dimers. Pairs of dimers further coalesce in an anti-parallel orientation to form tetramers. These early stages of intermediate filament assembly can be accomplished solely by the central α-helices. By contrast, the assembly of tetramers into mature intermediate filaments is reliant upon an N-terminal head domain. IF head domains measure roughly 100 amino acids in length and have long been understood to exist in a state of structural disorder. Here, we describe experiments favoring the unexpected idea that head domains self-associate to form transient structural order in the form of labile cross-β interactions. We propose that this weak form of protein structure allows for dynamic regulation of IF assembly and disassembly. We further offer that what we have learned from studies of IF head domains may represent a simple, unifying template for understanding how thousands of other intrinsically disordered proteins help to establish dynamic morphological order within eukaryotic cells.
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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.