ArticleJournal of molecular biology2011
Slow myosin ATP turnover in the super-relaxed state in tarantula muscle.
Article in Journal of molecular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.
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Who cites it
56 citing papers in PubMed, 80 citations in OpenAlex.
- Modulating the myosin super-relaxed state as a therapeutic strategy for myosin light chain-linked cardiomyopathies.Biophysical reviews · 2026Review
- CaJournal of molecular and cellular cardiology · 2025Article
- Myosin relaxation states in skeletal muscle fibers of rats and mice: Effects of sex and adiposity.Physiological reports · 2025Article
- Reassessing the unifying hypothesis for hypercontractility caused by myosin mutations in hypertrophic cardiomyopathy.The EMBO journal · 2024Review
- Myosin folding boosts solubility in cardiac muscle sarcomeres.JCI insight · 2024Article
- The biochemically defined super relaxed state of myosin-A paradox.The Journal of biological chemistry · 2024Article
- Structure of theInternational journal of molecular sciences · 2023Article
- Cooperative & competitive binding of anti-myosin tail antibodies revealed by super-resolution microscopy.Archives of biochemistry and biophysics · 2023Article
- Physical activity impacts resting skeletal muscle myosin conformation and lowers its ATP consumption.The Journal of general physiology · 2023Article
- Cryo-EM structure of the folded-back state of human β-cardiac myosin.Nature communications · 2023Article
- Cryo-EM structure of the folded-back state of human β-cardiac myosin.bioRxiv : the preprint server for biology · 2023Article
- Variants of the myosin interacting-heads motif.The Journal of general physiology · 2023Article
- Structure of the Flight Muscle Thick Filament from the Bumble Bee,International journal of molecular sciences · 2022Article
- Cardiac Sarcomere Signaling in Health and Disease.International journal of molecular sciences · 2022Review
- Interacting-heads motif explains the X-ray diffraction pattern of relaxed vertebrate skeletal muscle.Biophysical journal · 2022Article
- Structural basis of the super- and hyper-relaxed states of myosin II.The Journal of general physiology · 2022Review
- Two Classes of Myosin Inhibitors, Para-nitroblebbistatin and Mavacamten, Stabilize β-Cardiac Myosin in Different Structural and Functional States.Journal of molecular biology · 2021Article
- Relaxed tarantula skeletal muscle has two ATP energy-saving mechanisms.The Journal of general physiology · 2021Article
- Convergent evolutionary pathways toward energy saving in muscle?The Journal of general physiology · 2021Article
- Cardiac myosin super relaxation (SRX): a perspective on fundamental biology, human disease and therapeutics.Biology open · 2021Review
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
We measured the nucleotide turnover rate of myosin in tarantula leg muscle fibers by observing single turnovers of the fluorescent nucleotide analog 2'-/3'-O-(N'-methylanthraniloyl)adenosine-5'-O-triphosphate, as monitored by the decrease in fluorescence when 2'-/3'-O-(N'-methylanthraniloyl)adenosine-5'-O-triphosphate (mantATP) is replaced by ATP in a chase experiment. We find a multiexponential process with approximately two-thirds of the myosin showing a very slow nucleotide turnover time constant (∼30 min). This slow-turnover state is termed the super-relaxed state (SRX). If fibers are incubated in 2'-/3'-O-(N'-methylanthraniloyl)adenosine-5'-O-diphosphate and chased with ADP, the SRX is not seen, indicating that trinucleotide-relaxed myosins are responsible for the SRX. Phosphorylation of the myosin regulatory light chain eliminates the fraction of myosin with a very long lifetime. The data imply that the very long-lived SRX in tarantula fibers is a highly novel adaptation for energy conservation in an animal that spends extremely long periods of time in a quiescent state employing a lie-in-wait hunting strategy. The presence of the SRX measured here correlates well with the binding of myosin heads to the core of the thick filament in a structure known as the "interacting-heads motif," observed previously by electron microscopy. Both the structural array and the long-lived SRX require relaxed filaments or relaxed fibers, both are lost upon myosin phosphorylation, and both appear to be more stable in tarantula than in vertebrate skeletal or vertebrate cardiac preparations.
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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.