Evidence map›Paper›PMID 20923649›Full record

ArticleBiophysical journal2010

Quantitative analysis of actin turnover in Listeria comet tails: evidence for catastrophic filament turnover.

Hao Yuan Kueh, William M Brieher, Timothy J Mitchison

Abstract read
In one paragraph

Article in Biophysical journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
–field-weighted citation impact
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

15 citing papers in PubMed.

  1. Length control emerges from cytoskeletal network geometry.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  2. Length control emerges from cytoskeletal network geometry.bioRxiv : the preprint server for biology · 2023
    Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Mechanisms of actin disassembly.Molecular biology of the cell · 2013
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. 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

3 authors.

Hao Yuan KuehDepartment of Systems Biology, Harvard University, Cambridge, MA, USA. kueh@caltech.edu
William M Brieher
Timothy J Mitchison

Funding

GENETIC AND BIOCHEMICAL ANALYSIS OF CYTOKINESISR01GM023928 · NIGMS · UNIVERSITY OF CALIFORNIA SAN FRANCISCO · PI MITCHISON, TIMOTHY J · 1985 to 2010
$3.6M
Howard Hughes Medical InstituteNIGMS NIH HHS GM 23928NIGMS NIH HHS R01 GM023928
6 · The paper itself

Abstract

Rapid assembly and disassembly (turnover) of actin filaments in cytoplasm drives cell motility and shape remodeling. While many biochemical processes that facilitate filament turnover are understood in isolation, it remains unclear how they work together to promote filament turnover in cells. Here, we studied cellular mechanisms of actin filament turnover by combining quantitative microscopy with mathematical modeling. Using live cell imaging, we found that actin polymer mass decay in Listeria comet tails is very well fit by a simple exponential. By analyzing candidate filament turnover pathways using stochastic modeling, we found that exponential polymer mass decay is consistent with either slow treadmilling, slow Arp2/3-dissociation, or catastrophic bursts of disassembly, but is inconsistent with acceleration of filament turnover by severing. Imaging of single filaments in Xenopus egg extract provided evidence that disassembly by bursting dominates isolated filament turnover in a cytoplasmic context. Taken together, our results point to a pathway where filaments grow transiently from barbed ends, rapidly terminate growth to enter a long-lived stable state, and then undergo a catastrophic burst of disassembly. By keeping filament lengths largely constant over time, such catastrophic filament turnover may enable cellular actin assemblies to maintain their mechanical integrity as they are turning over.

Indexed as

Comet AssayActin CytoskeletonActin-Related Protein 2-3 ComplexActinsAnimalsCell ExtractsListeriaModels, BiologicalMolecular WeightOvumXenopus laevisActin-Related Protein 2-3 ComplexActinsCell Extracts

Identifiers

PMID20923649
PMCPMC3042591

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.