Cullin-3–dependent deregulation of ACTN1 represents a pathogenic mechanism in nemaline myopathy
Open accessAbstract
Nemaline myopathy is a congenital neuromuscular disorder characterized by muscle weakness, fiber atrophy and presence of nemaline bodies within myofibers. However, the understanding of underlying pathomechanisms is lacking. Recently, mutations in KBTBD13, KLHL40 and KLHL41, three substrate adaptors for the E3-ubiquitin ligase Cullin-3, have been associated with early-onset nemaline myopathies. We hypothesized that deregulation of Cullin-3 and its muscle protein substrates may be responsible for the disease development. Using Cullin-3 knockout mice, we identified accumulation of non-muscle alpha-Actinins (ACTN1 and ACTN4) in muscles of these mice, which we also observed in KBTBD13 patients. Our data reveal that proper regulation of Cullin-3 activity and ACTN1 levels is essential for normal muscle and neuromuscular junction development. While ACTN1 is naturally downregulated during myogenesis, its overexpression in C2C12 myoblasts triggered defects in fusion, myogenesis and acetylcholine receptor clustering; features that we characterized in Cullin-3 deficient mice. Taken together, our data highlight the importance for Cullin-3 mediated degradation of ACTN1 for muscle development, and indicate a new pathomechanism for the etiology of myopathies seen in Cullin-3 knockout mice and nemaline myopathy patients.
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The genes ACTN1 and PIEZO2 play important roles in muscle development and function.
“The genes of ACTN1 (Blondelle et al. 2019) and PIEZO2 (Delle Vedove et al. 2016) play important roles in muscle development and function.”
From Genomic Analyses Unveil Helmeted Guinea Fowl (<i>Numida meleagris</i>) Domestication in West Africa (2021) · cites this paper as Blondelle et al. 2019
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- Authors
- Blondelle, J., Tallapaka, K., Seto, J. T., Ghassemian, M., Clark, M., Laitila, J. M., Bournazos, A., Singer, J. D., & Lange, S.
- Affiliations
- University of California San Diego (US)
- Royal Children's Hospital (AU)
- University of Helsinki (FI)
- The University of Sydney (AU)
- Portland State University (US)
- Corresponding author
- Blondelle, Jordan
- Lange, Stephan
- ORCID
- Venue
- JCI Insight
- Published
- 2019-05-16
- Volume
- 4
- Issue
- 10
- ISSN
- 2379-3708 (ISSN-L)
- PMC
- PMC6542616
- OpenAlex
- W2939763083
- Cited by
- 26
- References
- 88
- Citations by year
- 2026: 3 · 2025: 4 · 2024: 4 · 2023: 4 · 2022: 3 · 2021: 5 · 2020: 3
- FWCI
- 0.91
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- JCI Insight (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- PDXScholar (Portland State University) (submittedVersion)
- eScholarship (California Digital Library) (submittedVersion)
- Funders
- National Institutes of Health (HL128457, NS047101, S10 OD016234,S10 OD021724)
- Muscular Dystrophy Association (515518)
- American Heart Association (17UFEL33520004)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
- Health Sciences › Medicine › Genetics › Neurogenetic and Muscular Disorders Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Genomics and Rare Diseases
- Keywords
- nemaline myopathy, CUL3, E3 ubiquitin ligase, ACTN1, alpha-actinin, ubiquitin-mediated proteolysis, myogenesis, myoblast fusion, acetylcholine receptor clustering, neuromuscular junction formation, nemaline bodies
- MeSH terms
- Actinin, Animals, Disease Models, Animal, Humans, Membrane Proteins, Muscle Proteins, Muscular Diseases, Mutation, Neuromuscular Junction, Myopathies, Nemaline, Mice, Knockout, Muscle, Skeletal, Gene Expression Regulation, Developmental, Muscle Weakness, Genetic Predisposition to Disease, Ubiquitin-Protein Ligases, Cullin Proteins, Mice
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