ArticleBiophysical journal2013
Different head environments in tarantula thick filaments support a cooperative activation process.
Article in Biophysical journal, 2013. 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.
- Structural basis of the super- and hyper-relaxed states of myosin II.The Journal of general physiology · 2022Review
- Relaxed tarantula skeletal muscle has two ATP energy-saving mechanisms.The Journal of general physiology · 2021Article
- The myosin interacting-heads motif present in live tarantula muscle explains tetanic and posttetanic phosphorylation mechanisms.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Through thick and thin: dual regulation of insect flight muscle and cardiac muscle compared.Journal of muscle research and cell motility · 2019Review
- Lessons from a tarantula: new insights into myosin interacting-heads motif evolution and its implications on disease.Biophysical reviews · 2018Review
- Interacting-heads motif has been conserved as a mechanism of myosin II inhibition since before the origin of animals.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Hypertrophic cardiomyopathy and the myosin mesa: viewing an old disease in a new light.Biophysical reviews · 2018Review
- Lessons from a tarantula: new insights into muscle thick filament and myosin interacting-heads motif structure and function.Biophysical reviews · 2017Review
- Article
- 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
- Conserved Intramolecular Interactions Maintain Myosin Interacting-Heads Motifs Explaining Tarantula Muscle Super-Relaxed State Structural Basis.Journal of molecular biology · 2016Article
- An approach to improve the resolution of helical filaments with a large axial rise and flexible subunits.Journal of structural biology · 2016Article
- Article
- Sequential myosin phosphorylation activates tarantula thick filament via a disorder-order transition.Molecular bioSystems · 2015Article
- Tarantula myosin free head regulatory light chain phosphorylation stiffens N-terminal extension, releasing it and blocking its docking back.Molecular bioSystems · 2015Article
- The role of super-relaxed myosin in skeletal and cardiac muscle.Biophysical reviews · 2015Article
- A method for 3D-reconstruction of a muscle thick filament using the tilt series images of a single filament electron tomogram.Journal of structural biology · 2014Article
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8 authors.
Funding
Abstract
Myosin filaments from many muscles are activated by phosphorylation of their regulatory light chains (RLCs). Structural analysis of relaxed tarantula thick filaments shows that the RLCs of the interacting free and blocked myosin heads are in different environments. This and other data suggested a phosphorylation mechanism in which Ser-35 of the free head is exposed and constitutively phosphorylated by protein kinase C, whereas the blocked head is hidden and unphosphorylated; on activation, myosin light chain kinase phosphorylates the monophosphorylated free head followed by the unphosphorylated blocked head, both at Ser-45. Our goal was to test this model of phosphorylation. Mass spectrometry of quickly frozen, intact muscles showed that only Ser-35 was phosphorylated in the relaxed state. The location of this constitutively phosphorylated Ser-35 was analyzed by immunofluorescence, using antibodies specific for unphosphorylated or phosphorylated Ser-35. In the relaxed state, myofibrils were labeled by anti-pSer-35 but not by anti-Ser-35, whereas in rigor, labeling was similar with both. This suggests that only pSer-35 is exposed in the relaxed state, while in rigor, Ser-35 is also exposed. In the interacting-head motif of relaxed filaments, only the free head RLCs are exposed, suggesting that the constitutive pSer-35 is on the free heads, consistent with the proposed mechanism.
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