Evidence map›Paper›PMID 40663102›Full record

ArticleThe Journal of cell biology2025

Nodal modulator (NOMO) is a force-bearing transmembrane protein required for muscle differentiation.

Brigitte S Naughton, Swapnil C Devarkar, Vanessa Todorow, Sunanda Mallik, Stacey Oxendine, Sanjana Junnarkar, Yuan Ren, Julien Berro, Janine Kirstein, Yong Xiong and 1 more

Abstract read
In one paragraph

Article in The Journal of cell biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
–field-weighted citation impact
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

4 citing papers in PubMed.

  1. Mechanical forces stimulate Golgi export.The Journal of cell biology · 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

11 authors.

Brigitte S NaughtonDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT, USA.ORCID 0000-0001-6233-3319
Swapnil C Devarkar *Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT, USA.ORCID 0000-0002-9271-243X
Vanessa Todorow *Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT, USA.ORCID 0000-0002-7861-2870
Sunanda MallikDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT, USA.ORCID 0000-0002-3825-3527
Stacey OxendineNational Institutes of Health Post-Bac Research Education Program for Biological & Biomedical Sciences, Yale University , New Haven, CT, USA.ORCID 0009-0006-3789-4337
Sanjana JunnarkarLeibniz Institute on Aging - Fritz-Lipmann-Institute , Jena, Germany.ORCID 0009-0004-8858-8802
Yuan RenDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT, USA.ORCID 0000-0001-7155-7664
Julien BerroDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT, USA.ORCID 0000-0002-9560-8646
Janine KirsteinLeibniz Institute on Aging - Fritz-Lipmann-Institute , Jena, Germany.ORCID 0000-0003-4990-2497
Yong XiongDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT, USA.ORCID 0000-0001-9625-9313
Christian SchliekerDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT, USA.ORCID 0000-0002-1237-4267

Funding

Bachmann-Strauss Dystonia FellowshipU.S. Department of Defense PR200788
6 · The paper itself

Abstract

The ER relies on membrane-shaping proteins to maintain a continuous network of sheets and tubules that host distinct biological processes. How this intricate structure of the ER membrane system is maintained under conditions of mechanical strain is incompletely understood. NOMO is an ER-resident transmembrane protein that contributes to ER morphology and is highly expressed in striated muscle. In this study, we identify a critical interface between distal Ig domains that enables NOMO to maintain ER morphology and bear mechanical forces. By incorporating two independent tension sensors in the luminal domain of NOMO, we demonstrate that NOMO assemblies experience forces in the single piconewton range, with a significant contribution from the identified interface. These newly defined features are important-if not indispensable-for myogenesis, as interface mutations affecting mechanosensitivity fail to restore the essential role of NOMO during myogenesis in a C2C12 differentiation model. Moreover, NOMO depletion impairs nematode motility, underscoring a broader functional importance in muscle physiology.

Indexed as

Cell DifferentiationMembrane ProteinsMuscle DevelopmentAnimalsCaenorhabditis elegansCell LineEndoplasmic ReticulumHumansMiceProtein DomainsMembrane Proteins

Identifiers

PMID40663102
PMCPMC12262048

What Socratic 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 Socratic graph.