ArticleFrontiers in physiology2013
Myosin binding protein-C slow: a multifaceted family of proteins with a complex expression profile in fast and slow twitch skeletal muscles.
Article in Frontiers in physiology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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32 citing papers in PubMed, 47 citations in OpenAlex.
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- Relationships Between Expressions and Variants of the Myosin-Binding Protein C1 Gene and Fatty Acid Composition in Longissimus Thoracis Muscle of Grazing Sonid Sheep.Food science & nutrition · 2025Article
- Sex-dependent and muscle-specific progression of the MYBPC1 E248K Myotrem myopathy in response to aging.JCI insight · 2025Article
- Pulsatile Myofilament Activity in Myotrem Myopathy Associated with Myogenic Tremor.International journal of molecular sciences · 2025Article
- Landscape of alternative splicing and polyadenylation during growth and development of muscles in pigs.Communications biology · 2024Article
- Functional role of myosin-binding protein H in thick filaments of developing vertebrate fast-twitch skeletal muscle.The Journal of general physiology · 2024Article
- Fast myosin binding protein C knockout in skeletal muscle alters length-dependent activation and myofilament structure.Communications biology · 2024Article
- Functional role of myosin-binding protein H in thick filaments of developing vertebrate fast-twitch skeletal muscle.bioRxiv : the preprint server for biology · 2024Article
- Unlocking the Role of sMyBP-C: A Key Player in Skeletal Muscle Development and Growth.bioRxiv : the preprint server for biology · 2023Article
- Etiology of genetic muscle disorders induced by mutations in fast and slow skeletal MyBP-C paralogs.Experimental & molecular medicine · 2023Review
- Comprehensive analysis of pre-mRNA alternative splicing regulated by m6A methylation in pig oxidative and glycolytic skeletal muscles.BMC genomics · 2022Article
- Alternative splicing diversifies the skeletal muscle transcriptome during prolonged spaceflight.Skeletal muscle · 2022Article
- Article
- Fast skeletal myosin-binding protein-C regulates fast skeletal muscle contraction.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Myosin Binding Protein-C Forms Amyloid-Like Aggregates In Vitro.International journal of molecular sciences · 2021Article
- Sarcomeric myopathies associated with tremor: new insights and perspectives.Journal of muscle research and cell motility · 2020Article
- Skeletal muscle: A review of molecular structure and function, in health and disease.Wiley interdisciplinary reviews. Systems biology and medicine · 2020Review
- Skeletal MyBP-C isoforms tune the molecular contractility of divergent skeletal muscle systems.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Heterozygous variants in MYBPC1 are associated with an expanded neuromuscular phenotype beyond arthrogryposis.Human mutation · 2019Article
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2 authors at 1 institution in 1 country.
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Abstract
Myosin Binding Protein-C slow (sMyBP-C) comprises a complex family of proteins expressed in slow and fast type skeletal muscles. Similar to its fast and cardiac counterparts, sMyBP-C functions to modulate the formation of actomyosin cross-bridges, and to organize and stabilize sarcomeric A- and M-bands. The slow form of MyBP-C was originally classified as a single protein, however several variants encoded by the single MYBPC1 gene have been recently identified. Alternative splicing of the 5' and 3' ends of the MYBPC1 transcript has led to the differential expression of small unique segments interspersed between common domains. In addition, the NH2-terminus of sMyBP-C undergoes complex phosphorylation. Thus, alternative splicing and phosphorylation appear to regulate the functional activities of sMyBP-C. sMyBP-C proteins are not restricted to slow twitch muscles, but they are abundantly expressed in fast twitch muscles, too. Using bioinformatic tools, we herein perform a systematic comparison of the known human and mouse sMyBP-C variants. In addition, using single fiber westerns and antibodies to a common region of all known sMyBP-C variants, we present a detailed and comprehensive characterization of the expression profile of sMyBP-C proteins in the slow twitch soleus and the fast twitch flexor digitorum brevis (FDB) mouse muscles. Our studies demonstrate for the first time that distinct sMyBP-C variants are co-expressed in the same fiber, and that their expression profile differs among fibers. Given the differential expression of sMyBP-C variants in single fibers, it becomes apparent that each variant or combination thereof may play unique roles in the regulation of actomyosin cross-bridges formation and the stabilization of thick filaments.
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