ArticleBiophysical journal2003
Activation of the calcium-regulated thin filament by myosin strong binding.
Article in Biophysical journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 44 citations in OpenAlex.
- Desensitization of the Cardiac Troponin Complex by TnI Phosphorylation and Epigallocatechin-3-Gallate.ACS omega · 2026Article
- Tropomodulin-Tropomyosin Interplay Modulates Interaction Between Cardiac Myosin and Thin Filaments.Biomolecules · 2025Article
- Glutamate 139 of tropomyosin is critical for cardiac thin filament blocked-state stabilization.Journal of molecular and cellular cardiology · 2024Article
- Motility Assay to Probe the Calcium Sensitivity of Myosin and Regulated Thin Filaments.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Mechanisms of pathogenicity in the hypertrophic cardiomyopathy-associated TPM1 variant S215L.PNAS nexus · 2023Article
- MgADP Promotes Myosin Head Movement toward Actin at Low [CaInternational journal of molecular sciences · 2022Article
- CaAmerican journal of physiology. Cell physiology · 2020Article
- Fropofol decreases force development in cardiac muscle.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2018Article
- Structural determinants of muscle thin filament cooperativity.Archives of biochemistry and biophysics · 2016Review
- Using fluorescent myosin to directly visualize cooperative activation of thin filaments.The Journal of biological chemistry · 2015Article
- The myosin duty ratio tunes the calcium sensitivity and cooperative activation of the thin filament.Biochemistry · 2013Article
- Recent insights into muscle fatigue at the cross-bridge level.Frontiers in physiology · 2012Article
- Micromechanical thermal assays of Ca2+-regulated thin-filament function and modulation by hypertrophic cardiomyopathy mutants of human cardiac troponin.Journal of biomedicine & biotechnology · 2012Article
- Filament compliance influences cooperative activation of thin filaments and the dynamics of force production in skeletal muscle.PLoS computational biology · 2012Article
- The role of tropomyosin domains in cooperative activation of the actin-myosin interaction.Journal of molecular biology · 2011Article
- SPontaneous Oscillatory Contraction (SPOC): auto-oscillations observed in striated muscle at partial activation.Biophysical reviews · 2011Review
- Human actin mutations associated with hypertrophic and dilated cardiomyopathies demonstrate distinct thin filament regulatory properties in vitro.Journal of molecular and cellular cardiology · 2010Article
- The molecular effects of skeletal muscle myosin regulatory light chain phosphorylation.American journal of physiology. Regulatory, integrative and comparative physiology · 2009Article
- Close proximity of myosin loop 3 to troponin determined by triangulation of resonance energy transfer distance measurements.Biochemistry · 2009Article
- Regulatory light chain mutations associated with cardiomyopathy affect myosin mechanics and kinetics.Journal of molecular and cellular cardiology · 2009Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The current study was undertaken to investigate the relative contribution of calcium and myosin binding to thin filament activation. Using the in vitro motility assay, myosin strong binding to the thin filament was controlled by three mechanisms: 1), varying the myosin concentration of the motility surface, and adding either 2), inorganic phosphate (Pi) or 3), adenosine diphosphate (ADP) to the motility solutions. At saturating myosin conditions, Pi had no effect on thin filament motility. However, at subsaturating myosin concentrations, velocity was reduced at maximal and submaximal calcium in the presence of Pi. Adding ADP to the motility buffers reduced thin filament sliding velocity but increased the pCa(50) of the thin filament. Thus by limiting or increasing myosin strong binding (with the addition of Pi and ADP, respectively), the calcium concentration at which half maximal activation of the thin filament is achieved can be modulated. In experiments without ADP or Pi, the myosin concentration on the motility surface required to reach maximal velocity inversely correlated with the level of calcium activation. Through this approach, we demonstrate that myosin strong binding is essential for thin filament activation at both maximal and submaximal calcium levels, with the relative contribution of myosin strong binding being greatest at submaximal calcium. Furthermore, under conditions in which myosin strong binding is not rate limiting (i.e., saturating myosin conditions), our data suggest that a modulation of myosin cross-bridge kinetics is likely responsible for the graded response to calcium observed in the in vitro motility assay.
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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.