Evidence map›Paper›PMID 34880255›Full record

ArticleNature communications2021

Optogenetic relaxation of actomyosin contractility uncovers mechanistic roles of cortical tension during cytokinesis.

Kei Yamamoto, Haruko Miura, Motohiko Ishida, Yusuke Mii, Noriyuki Kinoshita, Shinji Takada, Naoto Ueno, Satoshi Sawai, Yohei Kondo, Kazuhiro Aoki

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
4.0field-weighted citation impact, top 5% 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

36 citing papers in PubMed, 52 citations in OpenAlex.

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  14. Engineering filamentous myosins for optical control of contractility.bioRxiv : the preprint server for biology · 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

10 authors at 2 institutions in 1 country.

Kei YamamotoNational Institute for Basic Biology, National Institutes of Natural Sciences, 5-1 Higashiyama, Myodaiji-cho, Okazaki, Aichi, 444-8787, Japan.ORCID http://orcid.org/0000-0003-2712-1550
Haruko MiuraNational Institute for Basic Biology, National Institutes of Natural Sciences, 5-1 Higashiyama, Myodaiji-cho, Okazaki, Aichi, 444-8787, Japan.
Motohiko IshidaGraduate School of Arts and Sciences, University of Tokyo, Komaba, 153-8902, Tokyo, Japan.
Yusuke MiiNational Institute for Basic Biology, National Institutes of Natural Sciences, 5-1 Higashiyama, Myodaiji-cho, Okazaki, Aichi, 444-8787, Japan.ORCID http://orcid.org/0000-0002-1907-5665
Noriyuki KinoshitaNational Institute for Basic Biology, National Institutes of Natural Sciences, 5-1 Higashiyama, Myodaiji-cho, Okazaki, Aichi, 444-8787, Japan.
Shinji TakadaNational Institute for Basic Biology, National Institutes of Natural Sciences, 5-1 Higashiyama, Myodaiji-cho, Okazaki, Aichi, 444-8787, Japan.ORCID http://orcid.org/0000-0003-4125-6056
Naoto UenoNational Institute for Basic Biology, National Institutes of Natural Sciences, 5-1 Higashiyama, Myodaiji-cho, Okazaki, Aichi, 444-8787, Japan.
Satoshi SawaiGraduate School of Arts and Sciences, University of Tokyo, Komaba, 153-8902, Tokyo, Japan.ORCID http://orcid.org/0000-0003-3764-219X
Yohei KondoNational Institute for Basic Biology, National Institutes of Natural Sciences, 5-1 Higashiyama, Myodaiji-cho, Okazaki, Aichi, 444-8787, Japan. y-kondo@nibb.ac.jp.
Kazuhiro AokiNational Institute for Basic Biology, National Institutes of Natural Sciences, 5-1 Higashiyama, Myodaiji-cho, Okazaki, Aichi, 444-8787, Japan. k-aoki@nibb.ac.jp.ORCID http://orcid.org/0000-0001-7263-1555
National Institute for Basic Biology · JPTokyo University of the Arts · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Actomyosin contractility generated cooperatively by nonmuscle myosin II and actin filaments plays essential roles in a wide range of biological processes, such as cell motility, cytokinesis, and tissue morphogenesis. However, subcellular dynamics of actomyosin contractility underlying such processes remains elusive. Here, we demonstrate an optogenetic method to induce relaxation of actomyosin contractility at the subcellular level. The system, named OptoMYPT, combines a protein phosphatase 1c (PP1c)-binding domain of MYPT1 with an optogenetic dimerizer, so that it allows light-dependent recruitment of endogenous PP1c to the plasma membrane. Blue-light illumination is sufficient to induce dephosphorylation of myosin regulatory light chains and a decrease in actomyosin contractile force in mammalian cells and Xenopus embryos. The OptoMYPT system is further employed to understand the mechanics of actomyosin-based cortical tension and contractile ring tension during cytokinesis. We find that the relaxation of cortical tension at both poles by OptoMYPT accelerated the furrow ingression rate, revealing that the cortical tension substantially antagonizes constriction of the cleavage furrow. Based on these results, the OptoMYPT system provides opportunities to understand cellular and tissue mechanics.

Indexed as

OptogeneticsActin CytoskeletonActomyosinAnimalsCell MembraneCell MovementCytokinesisCytoskeletal ProteinsDogsFemaleIntercellular JunctionsMadin Darby Canine Kidney CellsMaleMechanical PhenomenaMorphogenesisMuscle ContractionActomyosinCytoskeletal ProteinsMyosin-Light-Chain PhosphataseMyosin Type IIPPP1R12A protein, human

Identifiers

PMID34880255
PMCPMC8654997
OpenAlexW4226062205

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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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.