ArticleCurrent biology : CB2012
Membrane-bound myo1c powers asymmetric motility of actin filaments.
Article in Current biology : CB, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
41 citing papers in PubMed, 74 citations in OpenAlex.
- A method for reconstituting the motility of membrane-bound myosin on the surface of the cell-sized W/O droplet.MethodsX · 2026Article
- Pathogenic mechanism of the PLS1 gene variant in hearing loss and functional validation in a zebrafish model.Scientific reports · 2026Article
- Elucidating chiral myosin-induced actin dynamics: From single-filament behavior to collective structures.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Physiological roles of phosphoinositides and inositol phosphates: Implications for metabolic dysfunction-associated steatotic liver disease.Clinical science (London, England : 1979) · 2025Review
- Coupling between the lever arm and active site via an N-terminal extension tunes force sensitivity in the myosin-1 family.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.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
- The actomyosin system is essential for the integrity of the endosomal system in bloodstream formeLife · 2024Article
- Membrane-bound myosin IC drives the chiral rotation of the gliding actin filament around its longitudinal axis.Scientific reports · 2023Article
- Actin polymerisation and crosslinking drive left-right asymmetry in single cell and cell collectives.Nature communications · 2023Article
- Twist response of actin filaments.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Bending actin filaments: twists of fate.Faculty reviews · 2023Review
- SMOC2 promotes aggressive behavior of fibroblast-like synoviocytes in rheumatoid arthritis through transcriptional and post-transcriptional regulating MYO1C.Cell death & disease · 2022Article
- Class I Myosins, molecular motors involved in cell migration and cancer.Cell adhesion & migration · 2022Article
- The membrane-actin linker ezrin acts as a sliding anchor.Science advances · 2022Article
- Review
- Functional Role of Class III Myosins in Hair Cells.Frontiers in cell and developmental biology · 2021Review
- Myosin 1b flattens and prunes branched actin filaments.Journal of cell science · 2020Article
- Unconventional Myosins: How Regulation Meets Function.International journal of molecular sciences · 2019Review
- Myosin 1b is an actin depolymerase.Nature communications · 2019Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Class I myosins are molecular motors that link cellular membranes to the actin cytoskeleton and play roles in membrane tension generation, membrane dynamics, and mechanosignal transduction. The widely expressed myosin-Ic (myo1c) isoform binds tightly to phosphatidylinositol 4,5-bisphosphate [PtdIns(4,5)P(2)] via a pleckstrin homology domain located in the myo1c tail, which is important for its proper cellular localization. In this study, we found that myo1c can power actin motility on fluid membranes composed of physiological concentrations of PtdIns(4,5)P(2) and that this motility is inhibited by high concentrations of anionic phospholipids. Strikingly, this motility occurs along curved paths in a counterclockwise direction (i.e., the actin filaments turn in leftward circles). A biotinylated myo1c construct containing only the motor domain and the lever arm anchored via streptavidin on a membrane containing biotinylated lipid can also generate asymmetric motility, suggesting that the tail domain is not required for the counterclockwise turning. We found that the ability to produce counterclockwise motility is not a universal characteristic of myosin-I motors, as membrane-bound myosin-Ia (myo1a) and myosin-Ib (myo1b) are able to power actin gliding, but the actin gliding has no substantial turning bias. This work reveals a possible mechanism for establishing asymmetry in relationship to the plasma membrane.
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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.