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

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.

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Publication Details

Journal
The Journal of Cell Biology
Published
2025-05-31
DOI
https://doi.org/10.1083/jcb.202505010
Citations
2
Primary Topic
Cellular Mechanics and Interactions
Type
article
Field-Weighted Citation Impact
2.30

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article

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

Christian Schlieker, Swapnil C. Devarkar, Sunanda Mallik, Janine Kirstein et al.
2 citations
The Journal of Cell Biology
Cellular Mechanics and Interactions
2.30
article

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

Christian Schlieker, Swapnil C. Devarkar, Sunanda Mallik, Janine Kirstein, Yong Xiong, Yuan Ren, Brigitte S. Naughton, Julien Berro, Vanessa Todorow, Stacey Oxendine, Sanjana Junnarkar
article en
2 citations

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.

The Journal of Cell BiologyVol. 224(9)
Schiller International University (FR), Yale University (US), Yale New Haven Health System (US), Leibniz Institute on Aging - Fritz Lipmann Institute (FLI) (DE), Friedrich Schiller University Jena (DE)
U.S. Department of Defense, Yale University
Openalex Percentile: Top 12%
Cellular Mechanics and Interactions
2.30
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