Evidence map›Paper›PMID 24739159›Full record

ArticleBiophysical journal2014

Force generation by endocytic actin patches in budding yeast.

Anders E Carlsson, Philip V Bayly

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
2.9field-weighted citation impact, top 10% 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

40 citing papers in PubMed, 73 citations in OpenAlex.

  1. Article
  2. Article
  3. Cellular and Nuclear Forces: An Overview.Methods in molecular biology (Clifton, N.J.) · 2025
    Review
  4. Review
  5. Article
  6. Initial ciliary assembly inMolecular biology of the cell · 2023
    Article
  7. Article
  8. Endocytic proteins with prion-like domains form viscoelastic condensates that enable membrane remodeling.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  9. Value of models for membrane budding.Current opinion in cell biology · 2021
    Review
  10. Article
  11. Article
  12. Review
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. AP3M harbors actin filament binding activity that is crucial for vacuole morphology and stomatal closure inProceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  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

2 authors at 1 institution in 1 country.

Anders E CarlssonDepartment of Physics, Washington University, St. Louis, Missouri. Electronic address: aec@wustl.edu.
Philip V BaylyDepartment of Mechanical Engineering, Washington University, St. Louis, Missouri.
Washington University in St. Louis · US

Funding

Control of Actin Assembly and Cell Migration by Actin-Regulating ProteinsR01GM086882 · NIGMS · WASHINGTON UNIVERSITY · PI CARLSSON, ANDERS E · 2008 to 2011
$1.0M
NIGMS NIH HHS R01 GM086882NIGMS NIH HHS R01-GM086882
6 · The paper itself

Abstract

Membrane deformation during endocytosis in yeast is driven by local, templated assembly of a sequence of proteins including polymerized actin and curvature-generating coat proteins such as clathrin. Actin polymerization is required for successful endocytosis, but it is not known by what mechanisms actin polymerization generates the required pulling forces. To address this issue, we develop a simulation method in which the actin network at the protein patch is modeled as an active gel. The deformation of the gel is treated using a finite-element approach. We explore the effects and interplay of three different types of force driving invagination: 1), forces perpendicular to the membrane, generated by differences between actin polymerization rates at the edge of the patch and those at the center; 2), the inherent curvature of the coat-protein layer; and 3), forces parallel to the membrane that buckle the coat protein layer, generated by an actomyosin contractile ring. We find that with optimistic estimates for the stall stress of actin gel growth and the shear modulus of the actin gel, actin polymerization can generate almost enough force to overcome the turgor pressure. In combination with the other mechanisms, actin polymerization can the force over the critical value.

Indexed as

EndocytosisActinsActomyosinBiomechanical PhenomenaComputer SimulationFinite Element AnalysisPolymerizationPressureSaccharomycetalesTime FactorsActinsActomyosin

Identifiers

PMID24739159
PMCPMC4008824
OpenAlexW1965894593

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.