Evidence map›Paper›PMID 35670664›Full record

ArticleeLife2022

A mechanism with severing near barbed ends and annealing explains structure and dynamics of dendritic actin networks.

Danielle Holz, Aaron R Hall, Eiji Usukura, Sawako Yamashiro, Naoki Watanabe, Dimitrios Vavylonis

Open access · goldAbstract read
In one paragraph

Article in eLife, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.7field-weighted citation impact, top 37% 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

5 citing papers in PubMed, 7 citations in OpenAlex.

  1. Microscopic and structural observations of actin filament capping and severing by cytochalasin D.Proceedings of the National Academy of Sciences of the United States of America · 2025
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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 2 institutions in 2 countries.

Danielle HolzDepartment of Physics, Lehigh University, Bethlehem, United States.ORCID 0000-0002-6179-2297
Aaron R HallDepartment of Physics, Lehigh University, Bethlehem, United States.
Eiji UsukuraLaboratory of Single-Molecule Cell Biology, Kyoto University, Kyoto, Japan.
Sawako YamashiroLaboratory of Single-Molecule Cell Biology, Kyoto University, Kyoto, Japan.
Naoki WatanabeLaboratory of Single-Molecule Cell Biology, Kyoto University, Kyoto, Japan.
Dimitrios VavylonisDepartment of Physics, Lehigh University, Bethlehem, United States.ORCID 0000-0003-1802-3262
Kyoto University · JPLehigh University · US

Funding

Modeling mechanisms in cytokinesis, cell polarization and motilityR35GM136372 · NIGMS · LEHIGH UNIVERSITY · PI Dimitrios Vavylonis · 2020 to 2026
$3.2M
Theoretical and experimental studies of distributed actin turnoverR01GM114201 · NIGMS · LEHIGH UNIVERSITY · PI VAVYLONIS, DIMITRIOS · 2016 to 2019
$1.1M
NIGMS NIH HHS R01 GM114201NIGMS NIH HHS R35 GM136372
6 · The paper itself

Abstract

Single molecule imaging has shown that part of actin disassembles within a few seconds after incorporation into the dendritic filament network in lamellipodia, suggestive of frequent destabilization near barbed ends. To investigate the mechanisms behind network remodeling, we created a stochastic model with polymerization, depolymerization, branching, capping, uncapping, severing, oligomer diffusion, annealing, and debranching. We find that filament severing, enhanced near barbed ends, can explain the single molecule actin lifetime distribution, if oligomer fragments reanneal to free ends with rate constants comparable to in vitro measurements. The same mechanism leads to actin networks consistent with measured filament, end, and branch concentrations. These networks undergo structural remodeling, leading to longer filaments away from the leading edge, at the +/-35° orientation pattern. Imaging of actin speckle lifetimes at sub-second resolution verifies frequent disassembly of newly-assembled actin. We thus propose a unified mechanism that fits a diverse set of basic lamellipodia phenomenology.

Indexed as

ActinsCytoskeletonActin CytoskeletonPolymerizationPseudopodiaActinsactin polymerizationcell biologycell motilitycomputational modelinglamellipodiumphysics of living systemsxenopus

Identifiers

PMID35670664
PMCPMC9252579
OpenAlexW4281760216

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.