ArticleThe Journal of general physiology2019
The central role of the tail in switching off 10S myosin II activity.
Article in The Journal of general physiology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 21 citations in OpenAlex.
- Role of the nonhelical tailpiece of myosin-II in regulating filament architecture and function.The Journal of cell biology · 2026Article
- Structural basis of nonmuscle myosin-2 autoinhibition mechanisms.Nature communications · 2026Article
- "QuickStainer": a rapid negative staining device for improved preservation of molecular structure.Journal of structural biology · 2026Article
- Structure of the Myosin Thick Filaments in Muscle.Sub-cellular biochemistry · 2026Review
- Structural basis of nonmuscle myosin-2 autoinhibition mechanisms.bioRxiv : the preprint server for biology · 2025Article
- Structure of the Inhibited Smooth Muscle Myosin and Its Implications on the Regulation of Insect Striated Muscle Myosin.Life (Basel, Switzerland) · 2025Review
- Non-Muscle Myosin II A: Friend or Foe in Cancer?International journal of molecular sciences · 2024Review
- Structure of mavacamten-free human cardiac thick filaments within the sarcomere by cryoelectron tomography.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Visualization of cardiac thick filament dynamics in ex vivo heart preparations.Journal of molecular and cellular cardiology · 2023Article
- Article
- Structural basis of the super- and hyper-relaxed states of myosin II.The Journal of general physiology · 2022Review
- Actomyosin Complex.Sub-cellular biochemistry · 2022Article
- Filament evanescence of myosin II and smooth muscle function.The Journal of general physiology · 2021Review
- Structure of the shutdown state of myosin-2.Nature · 2020Article
- Article
- Muscle myosins form folded monomers, dimers, and tetramers during filament polymerization in vitro.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Linking the Landscape ofCells · 2020Review
- The mesa trail and the interacting heads motif of myosin II.Archives of biochemistry and biophysics · 2020Article
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6 authors at 2 institutions in 1 country.
Funding
Abstract
Myosin II is a motor protein with two heads and an extended tail that plays an essential role in cell motility. Its active form is a polymer (myosin filament) that pulls on actin to generate motion. Its inactive form is a monomer with a compact structure (10S sedimentation coefficient), in which the tail is folded and the two heads interact with each other, inhibiting activity. This conformation is thought to function in cells as an energy-conserving form of the molecule suitable for storage as well as transport to sites of filament assembly. The mechanism of inhibition of the compact molecule is not fully understood. We have performed a 3-D reconstruction of negatively stained 10S myosin from smooth muscle in the inhibited state using single-particle analysis. The reconstruction reveals multiple interactions between the tail and the two heads that appear to trap ATP hydrolysis products, block actin binding, hinder head phosphorylation, and prevent filament formation. Blocking these essential features of myosin function could explain the high degree of inhibition of the folded form of myosin thought to underlie its energy-conserving function in cells. The reconstruction also suggests a mechanism for unfolding when myosin is activated by phosphorylation.
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