Evidence map›Paper›PMID 33589498›Full record

ArticleJournal of cell science2021

The formin inhibitor SMIFH2 inhibits members of the myosin superfamily.

Yukako Nishimura, Shidong Shi, Fang Zhang, Rong Liu, Yasuharu Takagi, Alexander D Bershadsky, Virgile Viasnoff, James R Sellers

Open access · hybridAbstract read
In one paragraph

Article in Journal of cell science, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.

0numbers the graph read from it
0cells of the map it votes in
60citing papers in PubMed
6.9field-weighted citation impact, top 2% 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

60 citing papers in PubMed, 98 citations in OpenAlex.

  1. Myosin II-independent contraction of actin filaments in membrane nanotubes.Proceedings of the National Academy of Sciences of the United States of America · 2026
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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

8 authors at 2 institutions in 3 countries.

Yukako NishimuraMechanobiology Institute (MBI), National University of Singapore, Singapore 117411, Singapore.
Shidong ShiMechanobiology Institute (MBI), National University of Singapore, Singapore 117411, Singapore.
Fang ZhangNational Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD 20892, USA.
Rong LiuNational Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD 20892, USA.
Yasuharu TakagiNational Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD 20892, USA.
Alexander D BershadskyMechanobiology Institute (MBI), National University of Singapore, Singapore 117411, Singapore.
Virgile ViasnoffMechanobiology Institute (MBI), National University of Singapore, Singapore 117411, Singapore.
James R SellersNational Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD 20892, USA.
National Institutes of Health · USNational University of Singapore · SG

Funding

Expression Studies of Other Unconventional MyosinsZIAHL004232 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI SELLERS, JAMES · 2009 to 2025
$11.7M
ROLE OF PHOSPHORYLATION AS A REGULATORY MECHANISM IN MUSCLE CONTRACTIONZ01HL001786 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI SELLERS, JAMES R. · 1985 to 2008
$601k
Intramural NIH HHS Z01 HL001786
6 · The paper itself

Abstract

The small molecular inhibitor of formin FH2 domains, SMIFH2, is widely used in cell biological studies. It inhibits formin-driven actin polymerization in vitro, but not polymerization of pure actin. It is active against several types of formin from different species. Here, we found that SMIFH2 inhibits retrograde flow of myosin 2 filaments and contraction of stress fibers. We further checked the effect of SMIFH2 on non-muscle myosin 2A and skeletal muscle myosin 2 in vitro, and found that SMIFH2 inhibits activity of myosin ATPase and the ability to translocate actin filaments in the gliding actin in vitro motility assay. Inhibition of non-muscle myosin 2A in vitro required a higher concentration of SMIFH2 compared with that needed to inhibit retrograde flow and stress fiber contraction in cells. We also found that SMIFH2 inhibits several other non-muscle myosin types, including bovine myosin 10, Drosophila myosin 7a and Drosophila myosin 5, more efficiently than it inhibits formins. These off-target inhibitions demand additional careful analysis in each case when solely SMIFH2 is used to probe formin functions. This article has an associated First Person interview with Yukako Nishimura, joint first author of the paper.

Indexed as

Actin CytoskeletonMyosinsActinsAnimalsCattleForminsActinsForminsMyosinsActin-activated ATPaseForminsIn vitro motility assayMyosinsOff-target inhibition

Identifiers

PMID33589498
PMCPMC8121067
OpenAlexW3132318166

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.