ArticleAmerican journal of physiology. Regulatory, integrative and comparative physiology2010
The direct molecular effects of fatigue and myosin regulatory light chain phosphorylation on the actomyosin contractile apparatus.
Article in American journal of physiology. Regulatory, integrative and comparative physiology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 37 citations in OpenAlex.
- Lactic acidosis: implications for human exercise performance.European journal of applied physiology · 2025Review
- Philament: A filament tracking program to quickly and accurately analyze in vitro motility assays.Biophysical reports · 2024Article
- 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
- The Sick and the Weak: Neuropathies/Myopathies in the Critically Ill.Physiological reviews · 2015Review
- Phosphorylation of myosin regulatory light chain has minimal effect on kinetics and distribution of orientations of cross bridges of rabbit skeletal muscle.American journal of physiology. Regulatory, integrative and comparative physiology · 2014Article
- Motor protein function in skeletal abdominal muscle of cachectic cancer patients.Journal of cellular and molecular medicine · 2014Article
- Myosin phosphorylation and force potentiation in skeletal muscle: evidence from animal models.Journal of muscle research and cell motility · 2013Review
- Mechanical properties of respiratory muscles.Comprehensive Physiology · 2013Review
- Comparison of orientation and rotational motion of skeletal muscle cross-bridges containing phosphorylated and dephosphorylated myosin regulatory light chain.The Journal of biological chemistry · 2013Article
- From cycling between coupled reactions to the cross-bridge cycle: mechanical power output as an integral part of energy metabolism.Metabolites · 2012Article
- Fluctuations in the skeletal muscle power-velocity relationship and interferon-γ after a muscle-damaging event in humans.Extreme physiology & medicine · 2012Article
- Exercise and heart failure in the elderly.Heart failure reviews · 2012Review
- Understanding cardiomyopathy phenotypes based on the functional impact of mutations in the myosin motor.Circulation research · 2012Review
- Recent insights into muscle fatigue at the cross-bridge level.Frontiers in physiology · 2012Article
- 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
- Effects of actin-myosin kinetics on the calcium sensitivity of regulated thin filaments.The Journal of biological chemistry · 2010Article
- 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
5 authors at 2 institutions in 1 country.
Funding
Abstract
Skeletal muscle, during periods of exertion, experiences several different fatigue-based changes in contractility, including reductions in force, velocity, power output, and energy usage. The fatigue-induced changes in contractility stem from many different factors, including alterations in the levels of metabolites, oxidative damage, and phosphorylation of the myosin regulatory light chain (RLC). Here, we measured the direct molecular effects of fatigue-like conditions on actomyosin's unloaded sliding velocity using the in vitro motility assay. We examined how changes in ATP, ADP, P(i), and pH affect the ability of the myosin to translocate actin and whether the effects of each individual molecular species are additive. We found that the primary causes of the reduction in unloaded sliding velocity are increased [ADP] and lowered pH and that the combined effects of the molecular species are nonadditive. Furthermore, since an increase in RLC phosphorylation is often associated with fatigue, we examined the differential effects of myosin RLC phosphorylation and fatigue on actin filament velocity. We found that phosphorylation of the RLC causes a 22% depression in sliding velocity. On the other hand, RLC phosphorylation ameliorates the slowing of velocity under fatigue-like conditions. We also found that phosphorylation of the myosin RLC increases actomyosin affinity for ADP, suggesting a kinetic role for RLC phosphorylation. Furthermore, we showed that ADP binding to skeletal muscle is load dependent, consistent with the existence of a load-dependent isomerization of the ADP bound state.
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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.