A fluorescent folding reporter uncovers myosin misfolding as a driver of Hypertrophic Cardiomyopathy
Renato ArneseiD, Philipp J. DexheimeriD, Beatriz Escobar-DonceliD, Lotta Krüger, Govinda Adhikari, Nina KrpaniD, Daria Sehr, Juliane Kley, Luiza DeszcziD, Anton MeinhartiD, Janine KirsteiniD, Tim ClauseniD
Abstract
Hypertrophic cardiomyopathy (HCM) is a fatal genetic disorder causing the thickening of ventricular walls in the heart muscle. While certain mutations in cardiac myosin deregulate ATPase activity, the pathology mechanism of most HCM mutations is not known. Here, by designing a fluorescent reporter to monitor myosin folding in cells, we uncovered a distinct class of HCM mutations that cause graded defects in myosin maturation. Using C. elegans as a disease model, we found that folding deficient HCM variants cause myofilament disruption, impaired motility, and reduced lifespan. Dietary restrictions resulted in a near-complete recovery from these detrimental defects by activating autophagy pathways through insulin/TOR signaling. In conclusion, our study identifies myosin misfolding as an important driver of HCM, revealing therapeutic opportunities to counteract muscle protein disorders.
02 /Specification & Classification
Click any tag to browse matching papers- Citations
- 0
- Organism
- Research Focus
- Approach
Reproducibility ledger
Nobody has reported trying to reproduce this paper yet. Did you replicate an experiment or run the code? Your report saves the next lab a week.
Sign in to file a reproducibility report.
Related papers
- Hypertrophic cardiomyopathy mutations at the folded-back sequestered β-cardiac myosin S1-S2 and S1-S1 interfaces release sequestered heads and increase myosin enzymatic activity
A. S. Adhikari, D. V. Trivedi, … K. M. Ruppel·bioRxiv·Jan 31, 2019
- Myosin motor domains carrying mutations implicated in early or late onset Hypertrophic Cardiomyopathy have similar properties
C. D. Vera, C. A. Johnson, … L. A. LEINWAND·bioRxiv·Aug 10, 2019
- Hypertrophic cardiomyopathy disease results from disparate impairments of cardiac myosin function and auto-inhibition
J. Robert-Paganin, D. Auguin, A. Houdusse·bioRxiv·May 17, 2018
- Beyond the myosin mesa: a potential unifying hypothesis on the underlying molecular basis of hyper-contractility caused by a majority of hypertrophic cardiomyopathy mutations
Suman Nag, Darshan V Trivedi, … James A Spudich·bioRxiv·Jul 24, 2016
- Hypertrophic cardiomyopathy mutations Y115H and E497D disrupt the folded-back state of human beta-cardiac myosin allosterically
Neha Nandwani, Debanjan Bhowmik, … Kathleen M. Ruppel·Nature CommunicationsPeer-reviewed·Oct 1, 2025
- A myosin hypertrophic cardiomyopathy mutation disrupts the super-relaxed state and boosts contractility by enhanced actin attachment
Robert C. Cail, Bipasha Barua, … E. Michael Ostap·Proceedings of the National Academy of SciencesPeer-reviewed·Dec 24, 2025