ArticleThe Biochemical journal1997
Troponin I and troponin T interact with troponin C to produce different Ca2+-dependent effects on actin-tropomyosin filament motility.
Article in The Biochemical journal, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 42 citations in OpenAlex.
- The intrinsically disordered C terminus of troponin T binds to troponin C to modulate myocardial force generation.The Journal of biological chemistry · 2019Article
- The homozygous K280N troponin T mutation alters cross-bridge kinetics and energetics in human HCM.The Journal of general physiology · 2019Article
- Myopathy-inducing mutation H40Y in ACTA1 hampers actin filament structure and function.Biochimica et biophysica acta · 2016Article
- Muscle weakness in TPM3-myopathy is due to reduced Ca2+-sensitivity and impaired acto-myosin cross-bridge cycling in slow fibres.Human molecular genetics · 2015Article
- Mutations in repeating structural motifs of tropomyosin cause gain of function in skeletal muscle myopathy patients.Human molecular genetics · 2013Article
- The kinetics of mechanically coupled myosins exhibit group size-dependent regimes.Biophysical journal · 2013Article
- Interaction between troponin and myosin enhances contractile activity of myosin in cardiac muscle.DNA and cell biology · 2011Article
- Molecular mechanism of the E99K mutation in cardiac actin (ACTC Gene) that causes apical hypertrophy in man and mouse.The Journal of biological chemistry · 2011Article
- Investigation of changes in skeletal muscle alpha-actin expression in normal and pathological human and mouse hearts.Journal of muscle research and cell motility · 2010Article
- The direct molecular effects of fatigue and myosin regulatory light chain phosphorylation on the actomyosin contractile apparatus.American journal of physiology. Regulatory, integrative and comparative physiology · 2010Article
- The molecular effects of skeletal muscle myosin regulatory light chain phosphorylation.American journal of physiology. Regulatory, integrative and comparative physiology · 2009Article
- The molecular phenotype of human cardiac myosin associated with hypertrophic obstructive cardiomyopathy.Cardiovascular research · 2008Article
- The Delta 14 mutation of human cardiac troponin T enhances ATPase activity and alters the cooperative binding of S1-ADP to regulated actin.Biochemistry · 2004Article
- Regulatory proteins alter nucleotide binding to acto-myosin of sliding filaments in motility assays.Biophysical journal · 2003Article
- Random walks with thin filaments: application of in vitro motility assay to the study of actomyosin regulation.Journal of muscle research and cell motility · 2003Review
- Two mutations in troponin I that cause hypertrophic cardiomyopathy have contrasting effects on cardiac muscle contractility.The Biochemical journal · 2002Article
- A simple method for measuring the relative force exerted by myosin on actin filaments in the in vitro motility assay: evidence that tropomyosin and troponin increase force in single thin filaments.The Biochemical journal · 2000Article
- Regulation of force and unloaded sliding speed in single thin filaments: effects of regulatory proteins and calcium.The Journal of physiology · 2000Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We have developed an in vitro motility assay to make a detailed quantitative analysis of Ca2+ control of skeletal-muscle troponin-tropomyosin control of actin-filament movement over immobilized myosin. Ca2+ regulates both filament velocity and the fraction of filaments that are motile. We have demonstrated that the two effects are due to separate interactions of troponin C with troponin I and troponin T. When 64nM of the complex actin-tropomyosin-troponin I-troponin C was added at pCa 5, more than 80% of filaments were moving and their velocity did not change. At pCa 9, more than 20% of the filaments were moving. When 20nM of the complex actin-tropomyosin-troponin T+troponin I+troponin C was added at pCa 5, filament motility remained high, whereas velocity increased. The 30% increase in velocity observed when troponin T was present was also observed when heavy meromyosin fragment 1 labelled with N-ethylmaleimide (NEM S-1) was added after actin-tropomyosin filaments. The NEM S-1 effect was not additive with the troponin T-dependent velocity increase. The pattern of motile behaviour is characteristic of myosin on silicone-treated glass and different from the behaviour on nitrocellulose-coated glass.
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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.