ArticleProceedings of the National Academy of Sciences of the United States of America2015
Skip residues modulate the structural properties of the myosin rod and guide thick filament assembly.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed, 61 citations in OpenAlex.
- Structural basis of nonmuscle myosin-2 autoinhibition mechanisms.Nature communications · 2026Article
- Multi-omics Insight into Cardiac Myofibril Remodeling in Post-Prandial Burmese Pythons.bioRxiv : the preprint server for biology · 2026Article
- Structural basis of nonmuscle myosin-2 autoinhibition mechanisms.bioRxiv : the preprint server for biology · 2025Article
- Secondary nucleation guided noncovalent synthesis of dendritic homochiral superstructures via growth on and from surface.Nature communications · 2024Article
- Structure, regulation, and mechanisms of nonmuscle myosin-2.Cellular and molecular life sciences : CMLS · 2024Review
- A Laing distal myopathy-associated proline substitution in the β-myosin rod perturbs myosin cross-bridging activity.The Journal of clinical investigation · 2024Article
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- Abnormal myosin post-translational modifications and ATP turnover time associated with human congenital myopathy-related RYR1 mutations.Acta physiologica (Oxford, England) · 2023Article
- Structure of the Flight Muscle Thick Filament from the Bumble Bee,International journal of molecular sciences · 2022Article
- Stability profile of vimentin rod domain.Protein science : a publication of the Protein Society · 2022Article
- The small molecule chemical compound cinobufotalin attenuates resistance to DDP by inducing ENKUR expression to suppress MYH9-mediated c-Myc deubiquitination in lung adenocarcinoma.Acta pharmacologica Sinica · 2022Article
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- Contiguity and Structural Impacts of a Non-Myosin Protein within the Thick Filament Myosin Layers.Biology · 2021Article
- Secondary Structure of the Novel Myosin Binding Domain WYR and Implications within Myosin Structure.Biology · 2021Article
- The SARS-CoV-2 SSHHPS Recognized by the Papain-like Protease.ACS infectious diseases · 2021Article
- The myosin II coiled-coil domain atomic structure in its native environment.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Filament evanescence of myosin II and smooth muscle function.The Journal of general physiology · 2021Review
- Evidence for S2 flexibility by direct visualization of quantum dot-labeled myosin heads and rods within smooth muscle myosin filaments moving on actin in vitro.The Journal of general physiology · 2021Article
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
Abstract
The rod of sarcomeric myosins directs thick filament assembly and is characterized by the insertion of four skip residues that introduce discontinuities in the coiled-coil heptad repeats. We report here that the regions surrounding the first three skip residues share high structural similarity despite their low sequence homology. Near each of these skip residues, the coiled-coil transitions to a nonclose-packed structure inducing local relaxation of the superhelical pitch. Moreover, molecular dynamics suggest that these distorted regions can assume different conformationally stable states. In contrast, the last skip residue region constitutes a true molecular hinge, providing C-terminal rod flexibility. Assembly of myosin with mutated skip residues in cardiomyocytes shows that the functional importance of each skip residue is associated with rod position and reveals the unique role of the molecular hinge in promoting myosin antiparallel packing. By defining the biophysical properties of the rod, the structures and molecular dynamic calculations presented here provide insight into thick filament formation, and highlight the structural differences occurring between the coiled-coils of myosin and the stereotypical tropomyosin. In addition to extending our knowledge into the conformational and biological properties of coiled-coil discontinuities, the molecular characterization of the four myosin skip residues also provides a guide to modeling the effects of rod mutations causing cardiac and skeletal myopathies.
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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.