ArticleProceedings of the National Academy of Sciences of the United States of America2014
A vertebrate myosin-I structure reveals unique insights into myosin mechanochemical tuning.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed.
- The structure of the native cardiac crossbridge in the rigor state.Science advances · 2026Article
- Myosin Class I Genes Follow a Cell Type-Specific Transcription Pattern in Human Haematopoietic Cell Lines.International journal of molecular sciences · 2026Article
- MYO1B in human disease: an actin-based motor linking membrane trafficking to oncogenic signaling, metastasis, and vascular aging.Frontiers in oncology · 2026Review
- A myosin hypertrophic cardiomyopathy mutation disrupts the super-relaxed state and boosts contractility by enhanced actin attachment.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Long-tailed class I myosins rely on tail-mediated phosphoinositide recognition for specific membrane recruitment.Cell communication and signaling : CCS · 2025Article
- High-resolution structures of Myosin-IC reveal a unique actin-binding orientation, ADP release pathway, and power stroke trajectory.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- High resolution structures of Myosin-IC reveal a unique actin-binding orientation, ADP release pathway, and power stroke trajectory.bioRxiv : the preprint server for biology · 2025Article
- Ensembles of human myosin-19 bound to calmodulin and regulatory light chain RLC12B drive multimicron transport.The Journal of biological chemistry · 2023Article
- Actomyosin Complex.Sub-cellular biochemistry · 2022Article
- Cardiomyopathy mutations impact the actin-activated power stroke of human cardiac myosin.Biophysical journal · 2021Article
- Alternative N-terminal regions ofThe Journal of biological chemistry · 2020Article
- Full-lengtheLife · 2020Article
- Conformational distributions of isolated myosin motor domains encode their mechanochemical properties.eLife · 2020Article
- Unconventional Myosins: How Regulation Meets Function.International journal of molecular sciences · 2019Review
- Dilated cardiomyopathy mutation in the converter domain of human cardiac myosin alters motor activity and response to omecamtiv mecarbil.The Journal of biological chemistry · 2019Article
- Atomistic Models from Orientation and Distance Constraints Using EPR of a Bifunctional Spin Label.Biophysical journal · 2019Article
- Converter domain mutations in myosin alter structural kinetics and motor function.The Journal of biological chemistry · 2019Article
- Structural and mechanistic insights into the function of the unconventional class XIV myosin MyoA fromProceedings of the National Academy of Sciences of the United States of America · 2018Article
- High-resolution cryo-EM structures of actin-bound myosin states reveal the mechanism of myosin force sensing.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- N-terminal splicing extensions of the humanThe Journal of biological chemistry · 2017Article
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Authors and funding
7 authors.
Funding
Abstract
Myosins are molecular motors that power diverse cellular processes, such as rapid organelle transport, muscle contraction, and tension-sensitive anchoring. The structural adaptations in the motor that allow for this functional diversity are not known, due, in part, to the lack of high-resolution structures of highly tension-sensitive myosins. We determined a 2.3-Å resolution structure of apo-myosin-Ib (Myo1b), which is the most tension-sensitive myosin characterized. We identified a striking unique orientation of structural elements that position the motor's lever arm. This orientation results in a cavity between the motor and lever arm that holds a 10-residue stretch of N-terminal amino acids, a region that is divergent among myosins. Single-molecule and biochemical analyses show that the N terminus plays an important role in stabilizing the post power-stroke conformation of Myo1b and in tuning the rate of the force-sensitive transition. We propose that this region plays a general role in tuning the mechanochemical properties of myosins.
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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.