ArticleBiochemistry2013
Regulatory light chain mutants linked to heart disease modify the cardiac myosin lever arm.
Article in Biochemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 26 citations in OpenAlex.
- Heterogeneous Dysregulation of Myosin Super-Relaxation and Energetics in Hypertrophic Cardiomyopathy.Circulation. Heart failure · 2025Article
- Phosphorylation Mimetic of Myosin Regulatory Light Chain Mitigates Cardiomyopathy-Induced Myofilament Impairment in Mouse Models of RCM and DCM.Life (Basel, Switzerland) · 2023Article
- In situ FRET-based localization of the N terminus of myosin binding protein-C in heart muscle cells.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Functional comparison of phosphomimetic S15D and T160D mutants of myosin regulatory light chain exchanged in cardiac muscle preparations of HCM and WT mice.Frontiers in cardiovascular medicine · 2022Article
- Hybrid method for representing ions in implicit solvation calculations.Computational and structural biotechnology journal · 2021Article
- Novel frameshift variant in MYL2 reveals molecular differences between dominant and recessive forms of hypertrophic cardiomyopathy.PLoS genetics · 2020Article
- Respiratory syncytial virus-associated mortality in a healthy 3-year-old child: a case report.BMC pediatrics · 2019Article
- 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
- Pseudophosphorylation of cardiac myosin regulatory light chain: a promising new tool for treatment of cardiomyopathy.Biophysical reviews · 2017Review
- Auxotonic to isometric contraction transitioning in a beating heart causes myosin step-size to down shift.PloS one · 2017Article
- Phosphorylation of the regulatory light chain of myosin in striated muscle: methodological perspectives.European biophysics journal : EBJ · 2016Review
- 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
- Novel familial dilated cardiomyopathy mutation in MYL2 affects the structure and function of myosin regulatory light chain.The FEBS journal · 2015Article
- Impact of familial hypertrophic cardiomyopathy-linked mutations in the NH2 terminus of the RLC on β-myosin cross-bridge mechanics.Journal of applied physiology (Bethesda, Md. : 1985) · 2014Article
- In vivo orientation of single myosin lever arms in zebrafish skeletal muscle.Biophysical journal · 2014Article
- Ventricular myosin modifies in vitro step-size when phosphorylated.Journal of molecular and cellular cardiology · 2014Article
- Techniques for assessing 3-D cell-matrix mechanical interactions in vitro and in vivo.Experimental cell research · 2013Review
- The Qdot-labeled actin super-resolution motility assay measures low-duty cycle muscle myosin step size.Biochemistry · 2013Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Myosin is the chemomechanical energy transducer in striated heart muscle. The myosin cross-bridge applies impulsive force to actin while consuming ATP chemical energy to propel myosin thick filaments relative to actin thin filaments in the fiber. Transduction begins with ATP hydrolysis in the cross-bridge driving rotary movement of a lever arm converting torque into linear displacement. Myosin regulatory light chain (RLC) binds to the lever arm and modifies its ability to translate actin. Gene sequencing implicated several RLC mutations in heart disease, and three of them are investigated here using photoactivatable GFP-tagged RLC (RLC-PAGFP) exchanged into permeabilized papillary muscle fibers. A single-lever arm probe orientation is detected in the crowded environment of the muscle fiber by using RLC-PAGFP with dipole orientation deduced from the three-spatial dimension fluorescence emission pattern of the single molecule. Symmetry and selection rules locate dipoles in their half-sarcomere, identify those at the minimal free energy, and specify active dipole contraction intermediates. Experiments were performed in a microfluidic chamber designed for isometric contraction, total internal reflection fluorescence detection, and two-photon excitation second harmonic generation to evaluate sarcomere length. The RLC-PAGFP reports apparently discretized lever arm orientation intermediates in active isometric fibers that on average produce the stall force. Disease-linked mutants introduced into RLC move intermediate occupancy further down the free energy gradient, implying lever arms rotate more to reach stall force because mutant RLC increases lever arm shear strain. A lower free energy intermediate occupancy involves a lower energy conversion efficiency in the fiber relating a specific myosin function modification to the disease-implicated mutant.
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