Evidence map›Paper›PMID 34323216›Full record

ArticleeLife2021

Structural heterogeneity of cellular K5/K14 filaments as revealed by cryo-electron microscopy.

Miriam S Weber, Matthias Eibauer, Suganya Sivagurunathan, Thomas M Magin, Robert D Goldman, Ohad Medalia

Open access · goldAbstract read
In one paragraph

Article in eLife, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.9field-weighted citation impact, top 9% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

19 citing papers in PubMed, 31 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Filament structure and subcellular organization of the bacterial intermediate filament-like protein crescentin.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  5. Article
  6. Article
  7. Review
  8. Vimentin regulates nuclear segmentation in neutrophils.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  9. Article
  10. Article
  11. Filament assembly of theNucleus (Austin, Tex.) · 2022
    Article
  12. Article
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  14. Article
  15. Article
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  17. Review
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 3 institutions in 3 countries.

Miriam S WeberDepartment of Biochemistry, University of Zurich, Zurich, Switzerland.ORCID 0000-0003-2125-8222
Matthias EibauerDepartment of Biochemistry, University of Zurich, Zurich, Switzerland.
Suganya SivagurunathanDepartment of Cell and Developmental Biology, Northwestern University Feinberg School of Medicine, Chicago, United States.
Thomas M MaginInstitute of Biology, University of Leipzig, Leipzig, Germany.
Robert D GoldmanDepartment of Cell and Developmental Biology, Northwestern University Feinberg School of Medicine, Chicago, United States.
Ohad MedaliaDepartment of Biochemistry, University of Zurich, Zurich, Switzerland.ORCID 0000-0003-0994-2937
University of Zurich · CHNorthwestern University · USLeipzig University · DE

Funding

Structural basis of the specific protein-protein interactions underlying IF assemP01GM096971 · NIGMS · NORTHWESTERN UNIVERSITY AT CHICAGO · PI DANUSER, GAUDENZ, GELFAND, VLADIMIR I · 2011 to 2021
$16.8M
Mechanobiology of Vimentin Intermediate Filaments in 3D Collective Cell MigrationR01GM140108 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI GUO, MING, WONG, IAN Y · 2021 to 2025
$2.3M
NIGMS NIH HHS P01 GM096971NIGMS NIH HHS R01 GM140108
6 · The paper itself

Abstract

Keratin intermediate filaments are an essential and major component of the cytoskeleton in epithelial cells. They form a stable yet dynamic filamentous network extending from the nucleus to the cell periphery, which provides resistance to mechanical stresses. Mutations in keratin genes are related to a variety of epithelial tissue diseases. Despite their importance, the molecular structure of keratin filaments remains largely unknown. In this study, we analyzed the structure of keratin 5/keratin 14 filaments within ghost mouse keratinocytes by cryo-electron microscopy and cryo-electron tomography. By averaging a large number of keratin segments, we have gained insights into the helical architecture of the filaments. Two-dimensional classification revealed profound variations in the diameter of keratin filaments and their subunit organization. Computational reconstitution of filaments of substantial length uncovered a high degree of internal heterogeneity along single filaments, which can contain regions of helical symmetry, regions with less symmetry and regions with significant diameter fluctuations. Cross-section views of filaments revealed that keratins form hollow cylinders consisting of multiple protofilaments, with an electron dense core located in the center of the filament. These findings shed light on the complex and remarkable heterogenic architecture of keratin filaments, suggesting that they are highly flexible, dynamic cytoskeletal structures.

Indexed as

AnimalsCryoelectron MicroscopyCytoskeletonEpithelial CellsIntermediate FilamentsKeratinocytesKeratinsMiceKeratinscell biologycryo-electron microscopycryo-electron tomographyintermediate filamentskeratin filamentsmolecular biophysicsmousestructural biology

Identifiers

PMID34323216
PMCPMC8360650
OpenAlexW3184972167

What OpenQuestion holds

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Registered trials

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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.