ArticleBiochemistry2007
Troponin T core structure and the regulatory NH2-terminal variable region.
Article in Biochemistry, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 55 citations in OpenAlex.
- Thin filament interaction and CaJournal of molecular and cellular cardiology · 2026Article
- Fine-tuning striated muscle performance: conserved sarcomere-level mechanisms across insect and vertebrate systems.Frontiers in physiology · 2026Review
- The highly conserved C-terminal end segment of troponin T binds tropomyosin and actin to function in modulating contractile kinetics.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Focus on cardiac troponin complex: From gene expression to cardiomyopathy.Genes & diseases · 2024Review
- Role of the interaction between troponin T and AMP deaminase by zinc bridge in modulating muscle contraction and ammonia production.Molecular and cellular biochemistry · 2024Review
- Alternative splicing diversifies the skeletal muscle transcriptome during prolonged spaceflight.Skeletal muscle · 2022Article
- Significance of Cardiac Troponins as an Identification Tool in COVID-19 Patients Using Biosensors: An Update.Frontiers in molecular biosciences · 2022Review
- The distal arthrogryposis-linked p.R63C variant promotes the stability and nuclear accumulation of TNNT3.Journal of clinical laboratory analysis · 2021Article
- Top-Down Proteomics Reveals Myofilament Proteoform Heterogeneity among Various Rat Skeletal Muscle Tissues.Journal of proteome research · 2020Article
- Comprehensive Characterization of Swine Cardiac Troponin T Proteoforms by Top-Down Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2018Article
- Clinically Divergent Mutation Effects on the Structure and Function of the Human Cardiac Tropomyosin Overlap.Biochemistry · 2017Article
- TNNT1, TNNT2, and TNNT3: Isoform genes, regulation, and structure-function relationships.Gene · 2016Review
- Protein Structure-Function Relationship at Work: Learning from Myopathy Mutations of the Slow Skeletal Muscle Isoform of Troponin T.Frontiers in physiology · 2016Review
- Historical perspective on heart function: the Frank-Starling Law.Biophysical reviews · 2015Review
- Abnormal splicing in the N-terminal variable region of cardiac troponin T impairs systolic function of the heart with preserved Frank-Starling compensation.Physiological reports · 2014Article
- Gene regulation, alternative splicing, and posttranslational modification of troponin subunits in cardiac development and adaptation: a focused review.Frontiers in physiology · 2014Review
- Troponin T nuclear localization and its role in aging skeletal muscle.Age (Dordrecht, Netherlands) · 2013Article
- The N-terminal extension of cardiac troponin T stabilizes the blocked state of cardiac thin filament.Biophysical journal · 2012Article
- Molecular effects of familial hypertrophic cardiomyopathy-related mutations in the TNT1 domain of cTnT.Journal of molecular biology · 2012Article
- The heart-specific NH2-terminal extension regulates the molecular conformation and function of cardiac troponin I.American journal of physiology. Heart and circulatory physiology · 2012Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
The conserved central and COOH-terminal regions of troponin T (TnT) interact with troponin C, troponin I, and tropomyosin to regulate striated muscle contraction. Phylogenic data show that the NH2-terminal region has evolved as an addition to the conserved core structure of TnT. This NH2-terminal region does not bind other thin filament proteins, and its sequence is hypervariable between fiber type and developmental isoforms. Previous studies have demonstrated that NH2-terminal modifications alter the COOH-terminal conformation of TnT and thin filament Ca2+-activation, yet the functional core structure of TnT and the mechanism of NH2-terminal modulation are not well understood. To define the TnT core structure and investigate the regulatory role of the NH2-terminal variable region, we investigated two classes of model TnT molecules: (1) NH2-terminal truncated cardiac TnT and (2) chimera proteins consisting of an acidic or basic skeletal muscle TnT NH2-terminus spliced to the cardiac TnT core. Deletion of the TnT hypervariable NH2-terminus preserved binding to troponin I and tropomyosin and sustained cardiac muscle contraction in the heart of transgenic mice. Further deletion of the conserved central region diminished binding to tropomyosin. The reintroduction of differently charged NH2-terminal domains in the chimeric molecules produced long-range conformational changes in the central and COOH-terminal regions to alter troponin I and tropomyosin binding. Similar NH2-terminal charge effects are demonstrated in naturally occurring cardiac TnT isoforms, indicating a physiological significance. These results suggest that the hypervariable NH2-terminal region modulates the conformation and function of the TnT core structure to fine-tune muscle contractility.
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