ArticleeLife2017
Cryo-EM structures reveal specialization at the myosin VI-actin interface and a mechanism of force sensitivity.
Article in eLife, 2017. 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, 80 citations in OpenAlex.
- Mutation-induced free-energy remodeling of recovery stroke and ATP hydrolysis in human cardiac β-myosin.Biophysical journal · 2026Article
- The structure of the native cardiac crossbridge in the rigor state.Science advances · 2026Article
- Tonotopic specialization of MYO7A isoforms in auditory hair cells.Nature communications · 2026Article
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- Actin isoform-specific interactions revealed byProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Unraveling Mutation-Induced Protein Communication Pathways in the Actomyosin Complex: Insights from Comprehensive Metadynamics Simulations.The journal of physical chemistry. B · 2025Article
- The role of the troponin T interactions with actin in regulation of cardiac thin filament revealed by the troponin T pathogenic variant Ile79Asn.Journal of molecular and cellular cardiology · 2025Article
- Histidine 73 methylation coordinates β-actin plasticity in response to key environmental factors.Nature communications · 2025Article
- Myosin forces elicit an F-actin structural landscape that mediates mechanosensitive protein recognition.bioRxiv : the preprint server for biology · 2024Article
- Insights into Actin Isoform-Specific Interactions with Myosin via Computational Analysis.Molecules (Basel, Switzerland) · 2024Article
- Sequence Alignment-Based Prediction of Myosin 7A: Structural Implications and Protein Interactions.International journal of molecular sciences · 2024Article
- Article
- Autoinhibition and activation of myosin VI revealed by its cryo-EM structure.Nature communications · 2024Article
- Conformational changes linked to ADP release from human cardiac myosin bound to actin-tropomyosin.The Journal of general physiology · 2023Article
- Myofilament-associated proteins with intrinsic disorder (MAPIDs) and their resolution by computational modeling.Quarterly reviews of biophysics · 2023Review
- Cryo-Electron Microscopy Reveals Cardiac Myosin Binding Protein-C M-Domain Interactions with the Thin Filament.Journal of molecular biology · 2022Article
- How gene duplication diversifies the landscape of protein oligomeric state and function.Current opinion in genetics & development · 2022Review
- Structural basis for tunable control of actin dynamics by myosin-15 in mechanosensory stereocilia.Science advances · 2022Article
- High-resolution structures of malaria parasite actomyosin and actin filaments.PLoS pathogens · 2022Article
- Discovery of ultrafast myosin, its amino acid sequence, and structural features.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
Despite extensive scrutiny of the myosin superfamily, the lack of high-resolution structures of actin-bound states has prevented a complete description of its mechanochemical cycle and limited insight into how sequence and structural diversification of the motor domain gives rise to specialized functional properties. Here we present cryo-EM structures of the unique minus-end directed myosin VI motor domain in rigor (4.6 Å) and Mg-ADP (5.5 Å) states bound to F-actin. Comparison to the myosin IIC-F-actin rigor complex reveals an almost complete lack of conservation of residues at the actin-myosin interface despite preservation of the primary sequence regions composing it, suggesting an evolutionary path for motor specialization. Additionally, analysis of the transition from ADP to rigor provides a structural rationale for force sensitivity in this step of the mechanochemical cycle. Finally, we observe reciprocal rearrangements in actin and myosin accompanying the transition between these states, supporting a role for actin structural plasticity during force generation by myosin VI.
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