ArticleProceedings of the National Academy of Sciences of the United States of America2015
Mechanochemical tuning of myosin-I by the N-terminal region.
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 31 papers.
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Who cites it
31 citing papers in PubMed, 46 citations in OpenAlex.
- Tonotopic specialization of MYO7A isoforms in auditory hair cells.Nature communications · 2026Article
- The unconventional regulation of non-muscle myosins.Biophysical reviews · 2026Article
- MYO1B in human disease: an actin-based motor linking membrane trafficking to oncogenic signaling, metastasis, and vascular aging.Frontiers in oncology · 2026Review
- 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
- Single-Molecule Investigation of Load-Dependent Actomyosin Dissociation Kinetics for Cardiac and Slow Skeletal Myosin.Small (Weinheim an der Bergstrasse, Germany) · 2024Article
- Myosin-1C differentially displaces tropomyosin isoforms altering their inhibition of motility.The Journal of biological chemistry · 2024Article
- Toward physics-based precision medicine: Exploiting protein dynamics to design new therapeutics and interpret variants.Protein science : a publication of the Protein Society · 2024Review
- The twoFrontiers in physiology · 2024Article
- Conformational changes linked to ADP release from human cardiac myosin bound to actin-tropomyosin.The Journal of general physiology · 2023Article
- Myosin motors in sensory hair bundle assembly.Current opinion in cell biology · 2022Review
- Deafness mutation in the MYO3A motor domain impairs actin protrusion elongation mechanism.Molecular biology of the cell · 2022Article
- Cardiomyopathy mutations impact the actin-activated power stroke of human cardiac myosin.Biophysical journal · 2021Article
- The actomyosin interface contains an evolutionary conserved core and an ancillary interface involved in specificity.Nature communications · 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
- Myosin-VIIa is expressed in multiple isoforms and essential for tensioning the hair cell mechanotransduction complex.Nature communications · 2020Article
- Myosin 1b is an actin depolymerase.Nature communications · 2019Article
- Atomistic Models from Orientation and Distance Constraints Using EPR of a Bifunctional Spin Label.Biophysical journal · 2019Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Myosins are molecular motors that generate force to power a wide array of motile cellular functions. Myosins have the inherent ability to change their ATPase kinetics and force-generating properties when they encounter mechanical loads; however, little is known about the structural elements in myosin responsible for force sensing. Recent structural and biophysical studies have shown that myosin-I isoforms, Myosin-Ib (Myo1b) and Myosin-Ic (Myo1c), have similar unloaded kinetics and sequences but substantially different responses to forces that resist their working strokes. Myo1b has the properties of a tension-sensing anchor, slowing its actin-detachment kinetics by two orders of magnitude with just 1 pN of resisting force, whereas Myo1c has the properties of a slow transporter, generating power without slowing under 1-pN loads that would stall Myo1b. To examine the structural elements that lead to differences in force sensing, we used single-molecule and ensemble kinetic techniques to show that the myosin-I N-terminal region (NTR) plays a critical role in tuning myosin-I mechanochemistry. We found that replacing the Myo1c NTR with the Myo1b NTR changes the identity of the primary force-sensitive transition of Myo1c, resulting in sensitivity to forces of <2 pN. Additionally, we found that the NTR plays an important role in stabilizing the post-power-stroke conformation. These results identify the NTR as an important structural element in myosin force sensing and suggest a mechanism for generating diversity of function among myosin isoforms.
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Registered trials
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.