ArticleBiophysical journal1998
Phosphorylation of myosin regulatory light chain eliminates force-dependent changes in relaxation rates in skeletal muscle.
Article in Biophysical journal, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed.
- Regulatory light chain phosphorylation augments length-dependent contraction in PTU-treated rats.The Journal of general physiology · 2019Article
- Influence of fascicle length on twitch potentiation of the medial gastrocnemius across three ankle angles.European journal of applied physiology · 2018Article
- Novel Sarcopenia-related Alterations in Sarcomeric Protein Post-translational Modifications (PTMs) in Skeletal Muscles Identified by Top-down Proteomics.Molecular & cellular proteomics : MCP · 2018Article
- Shortening speed dependent force potentiation is attenuated but not eliminated in skeletal muscles without myosin phosphorylation.Journal of muscle research and cell motility · 2017Article
- Myosin light chain phosphorylation is required for peak power output of mouse fast skeletal muscle in vitro.Pflugers Archiv : European journal of physiology · 2016Article
- Top-Down Targeted Proteomics Reveals Decrease in Myosin Regulatory Light-Chain Phosphorylation That Contributes to Sarcopenic Muscle Dysfunction.Journal of proteome research · 2016Article
- X-ray diffraction analysis of the effects of myosin regulatory light chain phosphorylation and butanedione monoxime on skinned skeletal muscle fibers.American journal of physiology. Cell physiology · 2016Article
- Rate-dependent force, intracellular calcium, and action potential voltage alternans are modulated by sarcomere length and heart failure induced-remodeling of thin filament regulation in human heart failure: A myocyte modeling study.Progress in biophysics and molecular biology · 2016Article
- Tri-modal regulation of cardiac muscle relaxation; intracellular calcium decline, thin filament deactivation, and cross-bridge cycling kinetics.Biophysical reviews · 2014Article
- Myosin phosphorylation and force potentiation in skeletal muscle: evidence from animal models.Journal of muscle research and cell motility · 2013Review
- Tetanic force potentiation of mouse fast muscle is shortening speed dependent.Journal of muscle research and cell motility · 2012Article
- Myosin light chain kinase and the role of myosin light chain phosphorylation in skeletal muscle.Archives of biochemistry and biophysics · 2011Review
- The effect of skeletal myosin light chain kinase gene ablation on the fatigability of mouse fast muscle.Journal of muscle research and cell motility · 2011Article
- Inhibitors of myosin, but not actin, alter transport through Tradescantia plasmodesmata.Protoplasma · 2011Article
- The direct molecular effects of fatigue and myosin regulatory light chain phosphorylation on the actomyosin contractile apparatus.American journal of physiology. Regulatory, integrative and comparative physiology · 2010Article
- Myosin regulatory light chain phosphorylation attenuates cardiac hypertrophy.The Journal of biological chemistry · 2008Article
- Acceleration of stretch activation in murine myocardium due to phosphorylation of myosin regulatory light chain.The Journal of general physiology · 2006Article
- Sarcomeric determinants of striated muscle relaxation kinetics.Pflugers Archiv : European journal of physiology · 2005Review
- Determinants of relaxation rate in rabbit skinned skeletal muscle fibres.The Journal of physiology · 2002Article
- Relaxation kinetics following sudden Ca(2+) reduction in single myofibrils from skeletal muscle.Biophysical journal · 2002Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
The rate of relaxation from steady-state force in rabbit psoas fiber bundles was examined before and after phosphorylation of myosin regulatory light chain (RLC). Relaxation was initiated using diazo-2, a photolabile Ca2+ chelator that has low Ca2+ binding affinity (K(Ca) = 4.5 x 10(5) M(-1)) before photolysis and high affinity (K(Ca) = 1.3 x 10(7) M(-1)) after photolysis. Before phosphorylating RLC, the half-times for relaxation initiated from 0.27 +/- 0.02, 0.51 +/- 0.03, and 0.61 +/- 0.03 Po were 90 +/- 6, 140 +/- 6, and 182 +/- 9 ms, respectively. After phosphorylation of RLC, the half-times for relaxation from 0.36 +/- 0.03 Po, 0.59 +/- 0.03 Po, and 0.65 +/- 0.02 Po were 197 +/- 35 ms, 184 +/- 35 ms, and 179 +/- 22 ms. This slowing of relaxation rates from steady-state forces less than 0.50 Po was also observed when bundles of fibers were bathed with N-ethylmaleimide-modified myosin S-1, a strongly binding cross-bridge derivative of S1. These results suggest that phosphorylation of RLC slows relaxation, most likely by slowing the apparent rate of transition of cross-bridges from strongly bound (force-generating) to weakly bound (non-force-generating) states, and reduces or eliminates Ca2+ and cross-bridge activation-dependent changes in relaxation rates.
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