Evidence map›Paper›PMID 30630946›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2019

High Rac1 activity is functionally translated into cytosolic structures with unique nanoscale cytoskeletal architecture.

Daniel J Marston, Karen L Anderson, Mark F Swift, Marie Rougie, Christopher Page, Klaus M Hahn, Niels Volkmann, Dorit Hanein

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
3.2field-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

24 citing papers in PubMed, 44 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. BioID Analysis of Actin-Binding Proteins.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  6. Reactivation of low avidity tumor-specific CD8Journal for immunotherapy of cancer · 2023
    Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Imaging Cytoskeleton Components by Electron Microscopy.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  15. Article
  16. Article
  17. Article
  18. Sculpting Dendritic Spines during Initiation and Maintenance of Neuropathic Pain.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2020
    Review
  19. Article
  20. Article
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

8 authors at 3 institutions in 1 country.

Daniel J MarstonDepartment of Pharmacology, The University of North Carolina at Chapel Hill, Chapel Hill, NC 27599.
Karen L AndersonBioinformatics and Structural Biology Program, Sanford Burnham Prebys Medical Discovery Institute, La Jolla, CA 92037.
Mark F SwiftBioinformatics and Structural Biology Program, Sanford Burnham Prebys Medical Discovery Institute, La Jolla, CA 92037.
Marie RougieDepartment of Pharmacology, The University of North Carolina at Chapel Hill, Chapel Hill, NC 27599.
Christopher PageBioinformatics and Structural Biology Program, Sanford Burnham Prebys Medical Discovery Institute, La Jolla, CA 92037.
Klaus M HahnDepartment of Pharmacology, The University of North Carolina at Chapel Hill, Chapel Hill, NC 27599.
Niels VolkmannBioinformatics and Structural Biology Program, Sanford Burnham Prebys Medical Discovery Institute, La Jolla, CA 92037 niels@burnham.org dorit@burnham.org.
Dorit HaneinBioinformatics and Structural Biology Program, Sanford Burnham Prebys Medical Discovery Institute, La Jolla, CA 92037 niels@burnham.org dorit@burnham.org.
Sanford Burnham Prebys Medical Discovery Institute · USUniversity of North Carolina at Chapel Hill · USDiscovery Institute · US

Funding

INTERACTIVE GRAPHICS FOR MOLECULAR STUDIES &MICROSCOPYP41EB002025 · NIBIB · UNIV OF NORTH CAROLINA CHAPEL HILL · PI SUPERFINE, RICHARD · 2003 to 2019
$16.9M
Ultrastructural Basis of Mechanotransduction in Matrix AdhesionsP01GM098412 · NIGMS · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI GROISMAN, ALEX · 2011 to 2015
$8.0M
Dissecting signaling in vivo via precise control and visualization of protein activityR35GM122596 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI Klaus M. Hahn · 2017 to 2026
$7.4M
Structural basis of allostery and mechanical properties of F-actinR01GM115972 · NIGMS · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI ALMO, STEVEN C., HANEIN, DORIT · 2016 to 2019
$2.3M
alpha-Catenin/F-actin Structure at Cell-Cell JunctionsR01GM119948 · NIGMS · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI HANEIN, DORIT, VOLKMANN, NIELS · 2017 to 2019
$1.9M
Tools for Quantitative Analysis of Complex Systems in CryoETP01GM121203 · NIGMS · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI VOLKMANN, NIELS · 2018 to 2019
$1.9M
Instrumentation Upgrade: acquisition of an intermediate voltage TEMS10OD012372 · OD · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI HANEIN, DORIT · 2012 to 2012
$1.9M
NIBIB NIH HHS P41 EB002025NIGMS NIH HHS P01 GM098412NIGMS NIH HHS P01 GM121203NIGMS NIH HHS R01 GM115972NIGMS NIH HHS R01 GM119948NIGMS NIH HHS R35 GM122596NIH HHS S10 OD012372
6 · The paper itself

Abstract

Rac1 activation is at the core of signaling pathways regulating polarized cell migration. So far, it has not been possible to directly explore the structural changes triggered by Rac1 activation at the molecular level. Here, through a multiscale imaging workflow that combines biosensor imaging of Rac1 dynamics with electron cryotomography, we identified, within the crowded environment of eukaryotic cells, a unique nanoscale architecture of a flexible, signal-dependent actin structure. In cell regions with high Rac1 activity, we found a structural regime that spans from the ventral membrane up to a height of ∼60 nm above that membrane, composed of directionally unaligned, densely packed actin filaments, most shorter than 150 nm. This unique Rac1-induced morphology is markedly different from the dendritic network architecture in which relatively short filaments emanate from existing, longer actin filaments. These Rac1-mediated scaffold assemblies are devoid of large macromolecules such as ribosomes or other filament types, which are abundant at the periphery and within the remainder of the imaged volumes. Cessation of Rac1 activity induces a complete and rapid structural transition, leading to the absence of detectable remnants of such structures within 150 s, providing direct structural evidence for rapid actin filament network turnover induced by GTPase signaling events. It is tempting to speculate that this highly dynamical nanoscaffold system is sensitive to local spatial cues, thus serving to support the formation of more complex actin filament architectures-such as those mandated by epithelial-mesenchymal transition, for example-or resetting the region by completely dissipating.

Indexed as

Actin CytoskeletonActinsAnimalsCell LineCell MovementCell PolarityCytoskeletonCytosolEpithelial-Mesenchymal TransitionGTP PhosphohydrolasesHumansMicerac1 GTP-Binding ProteinSignal TransductionActinsGTP Phosphohydrolasesrac1 GTP-Binding ProteinRAC1 protein, humanactin cytoskeletonbiosensorscellular cryotomographycorrelative imagingRho GTPase molecular signaling

Identifiers

PMID30630946
PMCPMC6347697
OpenAlexW2910699976

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.