Evidence map›Paper›PMID 23562268›Full record

ArticleCurrent biology : CB2013

NMII forms a contractile transcellular sarcomeric network to regulate apical cell junctions and tissue geometry.

Seham Ebrahim, Tomoki Fujita, Bryan A Millis, Elliott Kozin, Xuefei Ma, Sachiyo Kawamoto, Michelle A Baird, Michael Davidson, Shigenobu Yonemura, Yasuo Hisa and 4 more

Open access · bronzeAbstract read
In one paragraph

Article in Current biology : CB, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 115 papers.

0numbers the graph read from it
0cells of the map it votes in
115citing papers in PubMed
6.8field-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

115 citing papers in PubMed, 184 citations in OpenAlex.

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  20. Structure, regulation, and mechanisms of nonmuscle myosin-2.Cellular and molecular life sciences : CMLS · 2024
    Review

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

14 authors at 6 institutions in 2 countries.

Seham EbrahimLaboratory of Cell Structure and Dynamics, National Institute on Deafness and Other Communication Disorders, National Institutes of Health, Bethesda, MD 20892, USA.
Tomoki Fujita
Bryan A Millis
Elliott Kozin
Xuefei Ma
Sachiyo Kawamoto
Michelle A Baird
Michael Davidson
Shigenobu Yonemura
Yasuo Hisa
Mary Anne Conti
Robert S Adelstein
Hirofumi Sakaguchi
Bechara Kachar
National Heart Lung and Blood Institute · USKyoto Prefectural University of Medicine · JPNational Institutes of Health · USFlorida State University · USNational Institute on Deafness and Other Communication Disorders · USRIKEN Center for Computational Science · JP

Funding

Structural and Molecular Basis of Transduction in Auditory Sensory OrgansZIADC000002 · NIDCD · NATIONAL INSTITUTE ON DEAFNESS AND OTHER COMMUNICATION DISORDERS · PI KACHAR, BECHARA · 2009 to 2025
$38.3M
The Role of Nonmuscle Myosins in Development and DiseaseZIAHL004223 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI ADELSTEIN, ROBERT · 2009 to 2020
$7.1M
Alternative Splicing of Nonmuscle Myosin Heavy ChainsZIAHL004236 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI ADELSTEIN, ROBERT · 2009 to 2020
$5.7M
Molecular organization of intercellular junctions in the inner earZIADC000009 · NIDCD · NATIONAL INSTITUTE ON DEAFNESS AND OTHER COMMUNICATION DISORDERS · PI KACHAR, BECHARA · 2012 to 2020
$5.5M
In Vivo Function of Nonmuscle Myosin II-AZIAHL004218 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI ADELSTEIN, ROBERT · 2009 to 2019
$5.1M
The Role of Nonmuscle Myosin II in CytokinesisZIAHL004228 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI ADELSTEIN, ROBERT · 2009 to 2019
$5.0M
STRUCTURAL BASIS OF PERMEABILITY IN BLOOD-LABYRINTHINE &BLOOD-BRAIN BARRIERSZ01DC000009 · NIDCD · DEAFNESS &OTHER COMMUNICATION DISORDERS · PI KACHAR, B · 1992 to 1998
–
Intramural NIH HHS Z01 DC000009
6 · The paper itself

Abstract

Nonmuscle myosin II (NMII) is thought to be the master integrator of force within epithelial apical junctions, mediating epithelial tissue morphogenesis and tensional homeostasis. Mutations in NMII are associated with a number of diseases due to failures in cell-cell adhesion. However, the organization and the precise mechanism by which NMII generates and responds to tension along the intercellular junctional line are still not known. We discovered that periodic assemblies of bipolar NMII filaments interlace with perijunctional actin and α-actinin to form a continuous belt of muscle-like sarcomeric units (∼400-600 nm) around each epithelial cell. Remarkably, the sarcomeres of adjacent cells are precisely paired across the junctional line, forming an integrated, transcellular contractile network. The contraction/relaxation of paired sarcomeres concomitantly impacts changes in apical cell shape and tissue geometry. We show differential distribution of NMII isoforms across heterotypic junctions and evidence for compensation between isoforms. Our results provide a model for how NMII force generation is effected along the junctional perimeter of each cell and communicated across neighboring cells in the epithelial organization. The sarcomeric network also provides a well-defined target to investigate the multiple roles of NMII in junctional homeostasis as well as in development and disease.

Indexed as

Actin CytoskeletonActininActinsAnimalsHeterocyclic Compounds, 4 or More RingsIntercellular JunctionsMiceMicroscopy, FluorescenceMyosin Heavy ChainsMyosin Type IIOrgan of CortiRatsActininActinsblebbistatinHeterocyclic Compounds, 4 or More RingsMyh14 protein, mouseMyosin Heavy ChainsMyosin Type II

Identifiers

PMID23562268
PMCPMC3658137
OpenAlexW1995022882

What OpenQuestion holds

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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.