ArticleProceedings of the National Academy of Sciences of the United States of America2004
A point mutation in the regulatory light chain reduces the step size of skeletal muscle myosin.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 43 citations in OpenAlex.
- Myosin light chain proteins cooperatively promote sarcomere growth in fast-twitch muscle.Nature communications · 2026Article
- The elementary step that generates force and sinusoidal analysis in striated muscle fibers.Journal of muscle research and cell motility · 2025Review
- Article
- Mutations in MYLPF Cause a Novel Segmental Amyoplasia that Manifests as Distal Arthrogryposis.American journal of human genetics · 2020Article
- Opposing Pressures of Speed and Efficiency Guide the Evolution of Molecular Machines.Molecular biology and evolution · 2019Article
- 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
- 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
- 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
- A re-interpretation of the rate of tension redevelopment (k(TR)) in active muscle.Journal of muscle research and cell motility · 2013Article
- The Qdot-labeled actin super-resolution motility assay measures low-duty cycle muscle myosin step size.Biochemistry · 2013Article
- Mechanical coupling between myosin molecules causes differences between ensemble and single-molecule measurements.Biophysical journal · 2012Article
- Modification of interface between regulatory and essential light chains hampers phosphorylation-dependent activation of smooth muscle myosin.The Journal of biological chemistry · 2012Article
- Single myosin cross-bridge orientation in cardiac papillary muscle detects lever-arm shear strain in transduction.Biochemistry · 2011Article
- Visualizing key hinges and a potential major source of compliance in the lever arm of myosin.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Slow cardiac myosin regulatory light chain 2 (MYL2) was down-expressed in chronic heart failure patients.Clinical cardiology · 2011Article
- Cardiomyopathy-linked myosin regulatory light chain mutations disrupt myosin strain-dependent biochemistry.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Current evidence favors the theory that, when the globular motor domain of myosin attaches to actin, the light chain binding domain or "lever arm" rotates, and thereby generates movement of actin filaments. Myosin is uniquely designed for such a role in that a long alpha-helix (approximately 9 nm) extending from the C terminus of the catalytic core is stabilized by two calmodulin-like molecules, the regulatory light chain (RLC) and the essential light chain (ELC). Here, we introduce a single-point mutation into the skeletal myosin RLC, which results in a large (approximately 50%) reduction in actin filament velocity (V(actin)) without any loss in actin-activated MgATPase activity. Single-molecule analysis of myosin by optical trapping showed a comparable 2-fold reduction in unitary displacement or step size (d), without a significant change in the duration of the strongly attached state (tau(on)) after the power stroke. Assuming that V(actin) approximately d/tau(on), we can account for the change in velocity primarily by a change in the step size of the lever arm without incurring any change in the kinetic properties of the mutant myosin. These results suggest that a principal role for the many light chain isoforms in the myosin II class may be to modulate the flexural rigidity of the light chain binding domain to maximize tension development and movement during muscle contraction.
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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.