ArticleBiophysical journal2014
Three-dimensional organization of troponin on cardiac muscle thin filaments in the relaxed state.
Article in Biophysical journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed, 51 citations in OpenAlex.
- Structural changes in troponin during activation of skeletal and heart muscle determined in situ by polarised fluorescence.Biophysical reviews · 2024Review
- Glutamate 139 of tropomyosin is critical for cardiac thin filament blocked-state stabilization.Journal of molecular and cellular cardiology · 2024Article
- Clinical Biochemistry of Serum Troponin.Diagnostics (Basel, Switzerland) · 2024Review
- The correlation between high-sensitivity troponin-T and cell-free cardiac DNA in the blood of patients undergoing noncardiac, predominantly vascular surgery.The Journal of international medical research · 2024Observational
- Zebrafish as a model for cardiac disease; Cryo-EM structure of native cardiac thin filaments from Danio Rerio.Journal of muscle research and cell motility · 2023Article
- Structure and Dynamics of the Flexible Cardiac Troponin T Linker Domain in a Fully Reconstituted Thin Filament.Biochemistry · 2022Article
- The Mechanisms of Thin Filament Assembly and Length Regulation in Muscles.International journal of molecular sciences · 2022Review
- Hitting the Detection Limit in cAMP Signaling.Function (Oxford, England) · 2022Article
- The actin 'A-triad's' role in contractile regulation in health and disease.The Journal of physiology · 2020Review
- Troponin structure and function: a view of recent progress.Journal of muscle research and cell motility · 2020Review
- Docking Troponin T onto the Tropomyosin Overlapping Domain of Thin Filaments.Biophysical journal · 2020Article
- Cardiac muscle thin filament structures reveal calcium regulatory mechanism.Nature communications · 2020Article
- Age-Onset Phosphorylation of a Minor Actin Variant Promotes Intestinal Barrier Dysfunction.Developmental cell · 2019Article
- FRET-based analysis of the cardiac troponin T linker region reveals the structural basis of the hypertrophic cardiomyopathy-causing Δ160E mutation.The Journal of biological chemistry · 2019Article
- The Effect of Tropomyosin Mutations on Actin-Tropomyosin Binding: In Search of Lost Time.Biophysical journal · 2019Article
- After the revolution: how is Cryo-EM contributing to muscle research?Journal of muscle research and cell motility · 2019Review
- Moving beyond simple answers to complex disorders in sarcomeric cardiomyopathies: the role of integrated systems.Pflugers Archiv : European journal of physiology · 2019Review
- The missing links within troponin.Archives of biochemistry and biophysics · 2019Review
- Effects of cardiomyopathy-linked mutations K15N and R21H in tropomyosin on thin-filament regulation and pointed-end dynamics.Molecular biology of the cell · 2019Article
- Spontaneous transitions of actin-bound tropomyosin toward blocked and closed states.The Journal of general physiology · 2019Article
Corrections and comments
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Authors and funding
7 authors at 5 institutions in 3 countries.
Funding
Abstract
Muscle contraction is regulated by troponin-tropomyosin, which blocks and unblocks myosin binding sites on actin. To elucidate this regulatory mechanism, the three-dimensional organization of troponin and tropomyosin on the thin filament must be determined. Although tropomyosin is well defined in electron microscopy helical reconstructions of thin filaments, troponin density is mostly lost. Here, we determined troponin organization on native relaxed cardiac muscle thin filaments by applying single particle reconstruction procedures to negatively stained specimens. Multiple reference models led to the same final structure, indicating absence of model bias in the procedure. The new reconstructions clearly showed F-actin, tropomyosin, and troponin densities. At the 25 Å resolution achieved, troponin was considerably better defined than in previous reconstructions. The troponin density closely resembled the shape of troponin crystallographic structures, facilitating detailed interpretation of the electron microscopy density map. The orientation of troponin-T and the troponin core domain established troponin polarity. Density attributable to the troponin-I mobile regulatory domain was positioned where it could hold tropomyosin in its blocking position on actin, thus suggesting the underlying structural basis of thin filament regulation. Our previous understanding of thin filament regulation had been limited to known movements of tropomyosin that sterically block and unblock myosin binding sites on actin. We now show how troponin, the Ca(2+) sensor, may control these movements, ultimately determining whether muscle contracts or relaxes.
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