ArticleJournal of molecular biology2011
Role of the tail in the regulated state of myosin 2.
Article in Journal of molecular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
27 citing papers in PubMed.
- "QuickStainer": a rapid negative staining device for improved preservation of molecular structure.Journal of structural biology · 2026Article
- Nonmuscle myosin 2 without an assembly competence domain can incorporate into established filaments in cells.Molecular biology of the cell · 2025Article
- Reassessing the unifying hypothesis for hypercontractility caused by myosin mutations in hypertrophic cardiomyopathy.The EMBO journal · 2024Review
- Myosin folding boosts solubility in cardiac muscle sarcomeres.JCI insight · 2024Article
- Autoinhibition and activation of myosin VI revealed by its cryo-EM structure.Nature communications · 2024Article
- A simple and rapid preparation of smooth muscle myosin 2 for the electron microscopic analysis.Applied microscopy · 2024Article
- Ultra-thin membrane filter with a uniformly arrayed nanopore structure for nanoscale separation of extracellular vesicles without cake formation.Nanoscale advances · 2023Article
- Review on the structural understanding of the 10S myosin II in the era of Cryo-electron microscopy.Applied microscopy · 2022Article
- Article
- Structure of the shutdown state of myosin-2.Nature · 2020Article
- The mesa trail and the interacting heads motif of myosin II.Archives of biochemistry and biophysics · 2020Article
- The central role of the tail in switching off 10S myosin II activity.The Journal of general physiology · 2019Article
- Mammalian nonmuscle myosin II comes in three flavors.Biochemical and biophysical research communications · 2018Review
- Deciphering the super relaxed state of human β-cardiac myosin and the mode of action of mavacamten from myosin molecules to muscle fibers.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- 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
- Effect of ATP and regulatory light-chain phosphorylation on the polymerization of mammalian nonmuscle myosin II.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- The myosin mesa and the basis of hypercontractility caused by hypertrophic cardiomyopathy mutations.Nature structural & molecular biology · 2017Article
- Kinetic Adaptations of Myosins for Their Diverse Cellular Functions.Traffic (Copenhagen, Denmark) · 2016Review
- Various Themes of Myosin Regulation.Journal of molecular biology · 2016Review
Corrections and comments
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Authors and funding
8 authors.
Funding
Abstract
Myosin 2 from vertebrate smooth muscle or non-muscle sources is in equilibrium between compact, inactive monomers and thick filaments under physiological conditions. In the inactive monomer, the two heads pack compactly together, and the long tail is folded into three closely packed segments that are associated chiefly with one of the heads. The molecular basis of the folding of the tail remains unexplained. By using electron microscopy, we show that compact monomers of smooth muscle myosin 2 have the same structure in both the native state and following specific, intramolecular photo-cross-linking between Cys109 of the regulatory light chain (RLC) and segment 3 of the tail. Nonspecific cross-linking between lysine residues of the folded monomer by glutaraldehyde also does not perturb the compact conformation and stabilizes it against unfolding at high ionic strength. Sequence comparisons across phyla and myosin 2 isoforms suggest that the folding of the tail is stabilized by ionic interactions between the positively charged N-terminal sequence of the RLC and a negatively charged region near the start of tail segment 3 and that phosphorylation of the RLC could perturb these interactions. Our results support the view that interactions between the heads and the distal tail perform a critical role in regulating activity of myosin 2 molecules through stabilizing the compact monomer conformation.
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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.