Evidence map›Paper›PMID 33239610›Full record

ArticleNature communications2020

Biased localization of actin binding proteins by actin filament conformation.

Andrew R Harris, Pamela Jreij, Brian Belardi, Aaron M Joffe, Andreas R Bausch, Daniel A Fletcher

Open access · goldAbstract readVideo-Audio Media
In one paragraph

Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

28 citing papers in PubMed, 45 citations in OpenAlex.

  1. Article
  2. Article
  3. Myosin 2 - A general contractor for the cytoskeleton.Current opinion in cell biology · 2025
    Review
  4. Article
  5. Review
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Turn-On Protein Switches for Controlling Actin Binding in Cells.bioRxiv : the preprint server for biology · 2023
    Article
  17. Article
  18. Article
  19. Article
  20. Review
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 2 countries.

Andrew R HarrisDepartment of Bioengineering and Biophysics Program, University of California, Berkeley, 648 Stanley Hall MC 1762, Berkeley, CA, 94720, USA.
Pamela JreijDepartment of Bioengineering and Biophysics Program, University of California, Berkeley, 648 Stanley Hall MC 1762, Berkeley, CA, 94720, USA.
Brian BelardiDepartment of Bioengineering and Biophysics Program, University of California, Berkeley, 648 Stanley Hall MC 1762, Berkeley, CA, 94720, USA.
Aaron M JoffeDepartment of Bioengineering and Biophysics Program, University of California, Berkeley, 648 Stanley Hall MC 1762, Berkeley, CA, 94720, USA.
Andreas R BauschLehrstuhl für Biophysik (E27), Technische Universität München, Garching, 85748, Germany.
Daniel A FletcherDepartment of Bioengineering and Biophysics Program, University of California, Berkeley, 648 Stanley Hall MC 1762, Berkeley, CA, 94720, USA. fletch@berkeley.edu.ORCID 0000-0002-1890-5364
University of California, Berkeley · USLawrence Berkeley National Laboratory · USTechnical University of Munich · DE

Funding

Mechanical Regulation of Actin Binding ProteinsR01GM134137 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI FLETCHER, DANIEL A · 2019 to 2022
$1.5M
Investigating Tight Junction-Mediated Spatial Organization in Polarized Epithelia.F32GM115091 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI BELARDI, BRIAN · 2015 to 2017
$163k
NIGMS NIH HHS F32 GM115091NIGMS NIH HHS R01 GM134137
6 · The paper itself

Abstract

The assembly of actin filaments into distinct cytoskeletal structures plays a critical role in cell physiology, but how proteins localize differentially to these structures within a shared cytoplasm remains unclear. Here, we show that the actin-binding domains of accessory proteins can be sensitive to filament conformational changes. Using a combination of live cell imaging and in vitro single molecule binding measurements, we show that tandem calponin homology domains (CH1-CH2) can be mutated to preferentially bind actin networks at the front or rear of motile cells. We demonstrate that the binding kinetics of CH1-CH2 domain mutants varies as actin filament conformation is altered by perturbations that include stabilizing drugs and other binding proteins. These findings suggest that conformational changes of actin filaments in cells could help to direct accessory binding proteins to different actin cytoskeletal structures through a biophysical feedback loop.

Indexed as

Protein MultimerizationActin CytoskeletonActin Depolymerizing FactorsActinsAnimalsCytoplasmHEK293 CellsHeLa CellsHumansIntravital MicroscopyKineticsMicroscopy, FluorescenceMutationNeuropeptidesPoint MutationProtein BindingActin Depolymerizing FactorsActinsdrebrinsNeuropeptidesUTRN protein, humanUtrophin

Identifiers

PMID33239610
PMCPMC7688639
OpenAlexW3107595555

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.