Evidence map›Paper›PMID 31114072›Full record

ArticleNature materials2019

A mechano-signalling network linking microtubules, myosin IIA filaments and integrin-based adhesions.

Nisha Bte Mohd Rafiq, Yukako Nishimura, Sergey V Plotnikov, Visalatchi Thiagarajan, Zhen Zhang, Shidong Shi, Meenubharathi Natarajan, Virgile Viasnoff, Pakorn Kanchanawong, Gareth E Jones and 1 more

Erratum issuedOpen access · greenAbstract read
PubMed Publisher
In one paragraph

Article in Nature materials, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 94 papers.

0numbers the graph read from it
0cells of the map it votes in
94citing papers in PubMed
11.4field-weighted citation impact, top 1% 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

94 citing papers in PubMed, 178 citations in OpenAlex.

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  18. Tubulin Acetylation and the Cellular Mechanosensing and Stress Response.Results and problems in cell differentiation · 2025
    Review
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  20. Article

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

11 authors at 3 institutions in 4 countries.

Nisha Bte Mohd RafiqMechanobiology Institute, National University of Singapore, Singapore, Singapore.
Yukako NishimuraMechanobiology Institute, National University of Singapore, Singapore, Singapore.
Sergey V PlotnikovDepartment of Cell and Systems Biology, University of Toronto, Toronto, Ontario, Canada.
Visalatchi ThiagarajanMechanobiology Institute, National University of Singapore, Singapore, Singapore.
Zhen ZhangMechanobiology Institute, National University of Singapore, Singapore, Singapore.
Shidong ShiMechanobiology Institute, National University of Singapore, Singapore, Singapore.
Meenubharathi NatarajanMechanobiology Institute, National University of Singapore, Singapore, Singapore.
Virgile ViasnoffMechanobiology Institute, National University of Singapore, Singapore, Singapore.ORCID http://orcid.org/0000-0003-3949-2244
Pakorn KanchanawongMechanobiology Institute, National University of Singapore, Singapore, Singapore. biekp@nus.edu.sg.ORCID http://orcid.org/0000-0001-8765-3861
Gareth E JonesRandall Centre for Cell & Molecular Biophysics, King's College London, London, UK. gareth.jones@kcl.ac.uk.ORCID http://orcid.org/0000-0001-5879-3048
Alexander D BershadskyMechanobiology Institute, National University of Singapore, Singapore, Singapore. alexander.bershadsky@weizmann.ac.il.ORCID http://orcid.org/0000-0002-9571-7375
National University of Singapore · SGKing's College London · GBUniversity of Toronto · CA

Funding

Medical Research Council G1100041Medical Research Council MR/K015664/1
6 · The paper itself

Abstract

The interrelationship between microtubules and the actin cytoskeleton in mechanoregulation of integrin-mediated adhesions is poorly understood. Here, we show that the effects of microtubules on two major types of cell-matrix adhesion, focal adhesions and podosomes, are mediated by KANK family proteins connecting the adhesion protein talin with microtubule tips. Both total microtubule disruption and microtubule uncoupling from adhesions by manipulations with KANKs trigger a massive assembly of myosin IIA filaments, augmenting focal adhesions and disrupting podosomes. Myosin IIA filaments are indispensable effectors in the microtubule-driven regulation of integrin-mediated adhesions. Myosin IIA filament assembly depends on Rho activation by the RhoGEF GEF-H1, which is trapped by microtubules when they are connected with integrin-mediated adhesions via KANK proteins but released after their disconnection. Thus, microtubule capture by integrin-mediated adhesions modulates the GEF-H1-dependent effect of microtubules on the assembly of myosin IIA filaments. Subsequent actomyosin reorganization then remodels the focal adhesions and podosomes, closing the regulatory loop.

Indexed as

Adaptor Proteins, Signal TransducingApoptosis Regulatory ProteinsCarrier ProteinsCell Line, TumorCytoskeletal ProteinsFocal AdhesionsHumansIntegrinsMechanotransduction, CellularMicrotubulesNonmuscle Myosin Type IIAPodosomesRecombinant Proteinsrho-Associated Kinasesrho GTP-Binding ProteinsRho Guanine Nucleotide Exchange FactorsAdaptor Proteins, Signal TransducingApoptosis Regulatory ProteinsARHGEF2 protein, humanCarrier ProteinsCytoskeletal ProteinsIntegrinsKANK1 protein, humanKank2 protein, humanNonmuscle Myosin Type IIARecombinant Proteinsrho-Associated Kinasesrho GTP-Binding ProteinsRho Guanine Nucleotide Exchange FactorsTumor Suppressor Proteins

Identifiers

PMID31114072
OpenAlexW2945962537

What OpenQuestion holds

Textmetadata
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.