ArticleAmerican journal of physiology. Cell physiology2016
Reduced passive force in skeletal muscles lacking protein arginylation.
Article in American journal of physiology. Cell physiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 22 citations in OpenAlex.
- Mending the Achilles heels of titin in cardiac and musculoskeletal disease.Biophysical reviews · 2026Review
- An unbiased proteomic platform for ATE1-based arginylation profiling.Nature chemical biology · 2025Article
- Arginylation Regulates Cytoskeleton Organization and Cell Division and Affects Mitochondria in Fission Yeast.Molecular and cellular biology · 2022Article
- Sarcomere Length Nonuniformity and Force Regulation in Myofibrils and Sarcomeres.Biophysical journal · 2020Review
- Sarcomere length non-uniformities dictate force production along the descending limb of the force-length relation.Proceedings. Biological sciences · 2020Article
- The Axial Alignment of Titin on the Muscle Thick Filament Supports Its Role as a Molecular Ruler.Journal of molecular biology · 2020Article
- Extraction of Thick Filaments in Individual Sarcomeres Affects Force Production by Single Myofibrils.Biophysical journal · 2020Article
- Protein arginylation of cytoskeletal proteins in the muscle: modifications modifying function.American journal of physiology. Cell physiology · 2019Review
- Redox regulation of protein nanomechanics in health and disease: Lessons from titin.Redox biology · 2019Review
- Softening the Stressed Giant Titin in Diabetes Mellitus.Circulation research · 2018Article
- Thick Filament Protein Network, Functions, and Disease Association.Comprehensive Physiology · 2018Review
- Arginyltransferase ATE1 is targeted to the neuronal growth cones and regulates neurite outgrowth during brain development.Developmental biology · 2017Article
- Microfluidic perfusion shows intersarcomere dynamics within single skeletal muscle myofibrils.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Tampering with springs: phosphorylation of titin affecting the mechanical function of cardiomyocytes.Biophysical reviews · 2017Review
- Titin, a Central Mediator for Hypertrophic Signaling, Exercise-Induced Mechanosignaling and Skeletal Muscle Remodeling.Frontiers in physiology · 2016Review
Corrections and comments
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Authors and funding
12 authors at 4 institutions in 2 countries.
Funding
Abstract
Arginylation is a posttranslational modification that plays a global role in mammals. Mice lacking the enzyme arginyltransferase in skeletal muscles exhibit reduced contractile forces that have been linked to a reduction in myosin cross-bridge formation. The role of arginylation in passive skeletal myofibril forces has never been investigated. In this study, we used single sarcomere and myofibril measurements and observed that lack of arginylation leads to a pronounced reduction in passive forces in skeletal muscles. Mass spectrometry indicated that skeletal muscle titin, the protein primarily linked to passive force generation, is arginylated on five sites located within the A band, an important area for protein-protein interactions. We propose a mechanism for passive force regulation by arginylation through modulation of protein-protein binding between the titin molecule and the thick filament. Key points are as follows: 1) active and passive forces were decreased in myofibrils and single sarcomeres isolated from muscles lacking arginyl-tRNA-protein transferase (ATE1). 2) Mass spectrometry revealed five sites for arginylation within titin molecules. All sites are located within the A-band portion of titin, an important region for protein-protein interactions. 3) Our data suggest that arginylation of titin is required for proper passive force development in skeletal muscles.
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Registered trials
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 OpenQuestion graph.