ArticleBiochemistry2016
N-Terminus of Cardiac Myosin Essential Light Chain Modulates Myosin Step-Size.
Article in Biochemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 27 citations in OpenAlex.
- The structure of the native cardiac crossbridge in the rigor state.Science advances · 2026Article
- Modulating the myosin super-relaxed state as a therapeutic strategy for myosin light chain-linked cardiomyopathies.Biophysical reviews · 2026Review
- Functional role of myosin-binding protein H in thick filaments of developing vertebrate fast-twitch skeletal muscle.The Journal of general physiology · 2024Article
- Dual effect of N-terminal deletion of cardiac myosin essential light chain in mitigating cardiomyopathy.iScience · 2024Article
- Functional role of myosin-binding protein H in thick filaments of developing vertebrate fast-twitch skeletal muscle.bioRxiv : the preprint server for biology · 2024Article
- Native Top-Down Mass Spectrometry for Characterizing Sarcomeric Proteins Directly from Cardiac Tissue Lysate.Journal of the American Society for Mass Spectrometry · 2024Article
- Myosin essential light chain 1sa decelerates actin and thin filament gliding on β-myosin molecules.The Journal of general physiology · 2022Article
- Natural variant frequencies across domains from different sarcomere proteins cross-correlate to identify inter-protein contacts associated with cardiac muscle function and disease.Molecular biomedicine · 2021Article
- Cardiomyopathic mutations in essential light chain reveal mechanisms regulating the super relaxed state of myosin.The Journal of general physiology · 2021Article
- Insights into myosin regulatory and essential light chains: a focus on their roles in cardiac and skeletal muscle function, development and disease.Journal of muscle research and cell motility · 2020Article
- Ablation of the N terminus of cardiac essential light chain promotes the super-relaxed state of myosin and counteracts hypercontractility in hypertrophic cardiomyopathy mutant mice.The FEBS journal · 2020Article
- Hereditary heart disease: pathophysiology, clinical presentation, and animal models of HCM, RCM, and DCM associated with mutations in cardiac myosin light chains.Pflugers Archiv : European journal of physiology · 2019Review
- Cardiac and skeletal actin substrates uniquely tune cardiac myosin strain-dependent mechanics.Open biology · 2018Article
- Single cardiac ventricular myosins are autonomous motors.Open biology · 2018Article
- Hypercontractile mutant of ventricular myosin essential light chain leads to disruption of sarcomeric structure and function and results in restrictive cardiomyopathy in mice.Cardiovascular research · 2017Article
- In vitro actin motility velocity varies linearly with the number of myosin impellers.Archives of biochemistry and biophysics · 2017Article
- Auxotonic to isometric contraction transitioning in a beating heart causes myosin step-size to down shift.PloS one · 2017Article
- In vivo myosin step-size from zebrafish skeletal muscle.Open biology · 2016Article
- In vitro and in vivo single myosin step-sizes in striated muscle.Journal of muscle research and cell motility · 2015Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Muscle myosin cyclically hydrolyzes ATP to translate actin. Ventricular cardiac myosin (βmys) moves actin with three distinct unitary step-sizes resulting from its lever-arm rotation and with step-frequencies that are modulated in a myosin regulation mechanism. The lever-arm associated essential light chain (vELC) binds actin by its 43 residue N-terminal extension. Unitary steps were proposed to involve the vELC N-terminal extension with the 8 nm step engaging the vELC/actin bond facilitating an extra ∼19 degrees of lever-arm rotation while the predominant 5 nm step forgoes vELC/actin binding. A minor 3 nm step is the unlikely conversion of the completed 5 to the 8 nm step. This hypothesis was tested using a 17 residue N-terminal truncated vELC in porcine βmys (Δ17βmys) and a 43 residue N-terminal truncated human vELC expressed in transgenic mouse heart (Δ43αmys). Step-size and step-frequency were measured using the Qdot motility assay. Both Δ17βmys and Δ43αmys had significantly increased 5 nm step-frequency and coincident loss in the 8 nm step-frequency compared to native proteins suggesting the vELC/actin interaction drives step-size preference. Step-size and step-frequency probability densities depend on the relative fraction of truncated vELC and relate linearly to pure myosin species concentrations in a mixture containing native vELC homodimer, two truncated vELCs in the modified homodimer, and one native and one truncated vELC in the heterodimer. Step-size and step-frequency, measured for native homodimer and at two or more known relative fractions of truncated vELC, are surmised for each pure species by using a new analytical method.
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