Evidence map›Paper›PMID 19646871›Full record

ArticleCurrent biology : CB2009

Mechanosensing through cooperative interactions between myosin II and the actin crosslinker cortexillin I.

Yixin Ren, Janet C Effler, Melanie Norstrom, Tianzhi Luo, Richard A Firtel, Pablo A Iglesias, Ronald S Rock, Douglas N Robinson

Open access · bronzeAbstract read
In one paragraph

Article in Current biology : CB, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 99 papers.

0numbers the graph read from it
0cells of the map it votes in
99citing papers in PubMed
5.1field-weighted citation impact, top 4% 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

99 citing papers in PubMed, 141 citations in OpenAlex.

  1. Queue Gaps Among the IQGAPs inInternational journal of molecular sciences · 2026
    Review
  2. Opposing Activity at the Apical Surface: An Antagonistic Collaboration Between Crumbs and Myosin II Determines Organ Shape.BioEssays : news and reviews in molecular, cellular and developmental biology · 2026
    Review
  3. Models of Cellular Mechanosensation.Results and problems in cell differentiation · 2026
    Review
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  12. Viscoelasticity, Like Forces, Plays a Role in Mechanotransduction.Frontiers in cell and developmental biology · 2022
    Review
  13. Microtopographical guidance of macropinocytic signaling patches.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  14. Article
  15. Article
  16. The Unusual Suspects in Cytokinesis: Fitting the Pieces Together.Frontiers in cell and developmental biology · 2020
    Review
  17. Article
  18. Review
  19. Review
  20. Article

39 more citing papers are in PubMed but not listed here.

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

8 authors at 4 institutions in 1 country.

Yixin RenDepartment of Cell Biology, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.
Janet C Effler
Melanie Norstrom
Tianzhi Luo
Richard A Firtel
Pablo A Iglesias
Ronald S Rock
Douglas N Robinson
Johns Hopkins Medicine · USJohns Hopkins University · USUniversity of Chicago · USUniversity of California, San Diego · US

Funding

The Biochemical Basis for the Mechanics of CytokinesisR01GM066817 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI ROBINSON, DOUGLAS N · 2003 to 2025
$7.3M
Allostery in myosins studied at the molecular levelR01GM078450 · NIGMS · UNIVERSITY OF CHICAGO · PI ROCK, RONALD S · 2006 to 2015
$2.8M
NIGMS NIH HHS GM066817NIGMS NIH HHS GM078450NIGMS NIH HHS R01 GM066817NIGMS NIH HHS R01 GM078450
6 · The paper itself

Abstract

backgroundMechanosensing governs many processes from molecular to organismal levels, including during cytokinesis where it ensures successful and symmetrical cell division. Although many proteins are now known to be force sensitive, myosin motors with their ATPase activity and force-sensitive mechanical steps are well poised to facilitate cellular mechanosensing. For a myosin motor to experience tension, the actin filament must also be anchored.

resultsHere, we find a cooperative relationship between myosin II and the actin crosslinker cortexillin I where both proteins are essential for cellular mechanosensory responses. Although many functions of cortexillin I and myosin II are dispensable for cytokinesis, all are required for full mechanosensing. Our analysis demonstrates that this mechanosensor has three critical elements: the myosin motor where the lever arm acts as a force amplifier, a force-sensitive bipolar thick-filament assembly, and a long-lived actin crosslinker, which anchors the actin filament so that the motor may experience tension. We also demonstrate that a Rac small GTPase inhibits this mechanosensory module during interphase, allowing the module to be primarily active during cytokinesis.

conclusionsOverall, myosin II and cortexillin I define a cellular-scale mechanosensor that controls cell shape during cytokinesis. This system is exquisitely tuned through the enzymatic properties of the myosin motor, its lever arm length, and bipolar thick-filament assembly dynamics. The system also requires cortexillin I to stably anchor the actin filament so that the myosin motor can experience tension. Through this cross-talk, myosin II and cortexillin I define a cellular-scale mechanosensor that monitors and corrects shape defects, ensuring symmetrical cell division.

Indexed as

DictyosteliumMechanotransduction, CellularMicrofilament ProteinsModels, BiologicalMyosin Type IIPhosphorylationProtozoan Proteinsrac GTP-Binding ProteinsctxA protein, Dictyostelium discoideumMicrofilament ProteinsMyosin Type IIProtozoan ProteinsRacE protein, Dictyostelium discoideumrac GTP-Binding Proteins

Identifiers

PMID19646871
PMCPMC2763054
OpenAlexW2048056271

What OpenQuestion holds

Textmetadata
LicenceTDM
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.