Evidence map›Paper›PMID 38728140›Full record

ArticleCell reports2024

Two Septin complexes mediate actin dynamics during cell wound repair.

Viktor Stjepić, Mitsutoshi Nakamura, Justin Hui, Susan M Parkhurst

Abstract read
In one paragraph

Article in Cell reports, 2024. 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
–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

5 citing papers in PubMed.

  1. Mechanically-induced Septin Networks Protect Nuclear Integrity.bioRxiv : the preprint server for biology · 2026
    Article
  2. Article
  3. Article
  4. Septin complexes: Ahead of the curve.Cytoskeleton (Hoboken, N.J.) · 2025
    Article
  5. Actomyosin contraction in the follicular epithelium provides the major mechanical force for follicle rupture duringProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors.

Viktor StjepićBasic Sciences Division, Fred Hutchinson Cancer Center, Seattle, WA 98109, USA.
Mitsutoshi NakamuraBasic Sciences Division, Fred Hutchinson Cancer Center, Seattle, WA 98109, USA.
Justin HuiBasic Sciences Division, Fred Hutchinson Cancer Center, Seattle, WA 98109, USA.
Susan M ParkhurstBasic Sciences Division, Fred Hutchinson Cancer Center, Seattle, WA 98109, USA. Electronic address: susanp@fredhutch.org.

Funding

Translational Bioimaging Core Shared ResourceP30CA015704 · NCI · FRED HUTCHINSON CANCER RESEARCH CENTER · PI Eric Collisson · 1985 to 2026
$296.4M
Molecular and Cellular Mechanisms of Wound RepairR01GM111635 · NIGMS · FRED HUTCHINSON CANCER RESEARCH CENTER · PI PARKHURST, SUSAN M · 2015 to 2025
$4.8M
NCI NIH HHS P30 CA015704NIGMS NIH HHS R01 GM111635
6 · The paper itself

Abstract

Cells have robust wound repair systems to prevent further damage or infection and to quickly restore cell cortex integrity when exposed to mechanical and chemical stress. Actomyosin ring formation and contraction at the wound edge are major events during closure of the plasma membrane and underlying cytoskeleton during cell wound repair. Here, we show that all five Drosophila Septins are required for efficient cell wound repair. Based on their different recruitment patterns and knockdown/mutant phenotypes, two distinct Septin complexes, Sep1/Sep2/Pnut and Sep4/Sep5/Pnut, are assembled to regulate actin ring assembly, contraction, and remodeling during the repair process. Intriguingly, we find that these two Septin complexes have different F-actin bending activities. In addition, we find that Anillin regulates the recruitment of only one of two Septin complexes upon wounding. Our results demonstrate that two functionally distinct Septin complexes work side by side to discretely regulate actomyosin ring dynamics during cell wound repair.

Indexed as

ActinsDrosophila ProteinsSeptinsWound HealingActomyosinAnimalsCell Cycle ProteinsContractile ProteinsDrosophila melanogasterMicrofilament ProteinsActinsActomyosinCell Cycle ProteinsContractile ProteinsDrosophila ProteinsMicrofilament Proteinspnut protein, DrosophilaSep1 protein, DrosophilaSep2 protein, DrosophilaSep4 protein, DrosophilaSep5 protein, DrosophilaSeptinsactin bendingactin bundlingAnillincell wound repairCP: Cell biologycytoskeletonDrosophilaSeptins

Identifiers

PMID38728140
PMCPMC11203717

What OpenQuestion holds

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LicenceCC BY-NC
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.