ArticleThe Journal of cell biology2009
Coupled myosin VI motors facilitate unidirectional movement on an F-actin network.
Article in The Journal of cell biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
What it found
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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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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
34 citing papers in PubMed, 55 citations in OpenAlex.
- Organization of a cytoskeletal superstructure in the apical domain of intestinal tuft cells.The Journal of cell biology · 2024Article
- Small Peptide-Protein Interaction Pair for Genetically Encoded, Fixation Compatible Peptide-PAINT.Nano letters · 2021Article
- Unconventional Myosins: How Regulation Meets Function.International journal of molecular sciences · 2019Review
- Active cargo positioning in antiparallel transport networks.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Engaging myosin VI tunes motility, morphology and identity in endocytosis.Traffic (Copenhagen, Denmark) · 2018Article
- Differentiation between Oppositely Oriented Microtubules Controls Polarized Neuronal Transport.Neuron · 2017Review
- Acetylated Microtubules Are Preferentially Bundled Leading to Enhanced Kinesin-1 Motility.Biophysical journal · 2017Article
- KIF5A transports collagen vesicles of myofibroblasts during pleural fibrosis.Scientific reports · 2017Article
- Human myosin VIIa is a very slow processive motor protein on various cellular actin structures.The Journal of biological chemistry · 2017Article
- Structure analyses reveal a regulated oligomerization mechanism of the PlexinD1/GIPC/myosin VI complex.eLife · 2017Article
- Activated full-length myosin-X moves processively on filopodia with large steps toward diverse two-dimensional directions.Scientific reports · 2017Article
- Cargo Transport by Two Coupled Myosin Va Motors on Actin Filaments and Bundles.Biophysical journal · 2016Article
- Patterning protein complexes on DNA nanostructures using a GFP nanobody.Protein science : a publication of the Protein Society · 2016Article
- Kinetic Adaptations of Myosins for Their Diverse Cellular Functions.Traffic (Copenhagen, Denmark) · 2016Review
- A Robust Actin Filaments Image Analysis Framework.PLoS computational biology · 2016Article
- Clustering of a kinesin-14 motor enables processive retrograde microtubule-based transport in plants.Nature plants · 2015Article
- Cellular chirality arising from the self-organization of the actin cytoskeleton.Nature cell biology · 2015Article
- Article
- A Kinase Anchoring Protein 9 Is a Novel Myosin VI Binding Partner That Links Myosin VI with the PKA Pathway in Myogenic Cells.BioMed research international · 2015Article
- Motor coupling through lipid membranes enhances transport velocities for ensembles of myosin Va.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Unconventional myosins interact with the dense cortical actin network during processes such as membrane trafficking, cell migration, and mechanotransduction. Our understanding of unconventional myosin function is derived largely from assays that examine the interaction of a single myosin with a single actin filament. In this study, we have developed a model system to study the interaction between multiple tethered unconventional myosins and a model F-actin cortex, namely the lamellipodium of a migrating fish epidermal keratocyte. Using myosin VI, which moves toward the pointed end of actin filaments, we directly determine the polarity of the extracted keratocyte lamellipodium from the cell periphery to the cell nucleus. We use a combination of experimentation and simulation to demonstrate that multiple myosin VI molecules can coordinate to efficiently transport vesicle-size cargo over 10 microm of the dense interlaced actin network. Furthermore, several molecules of monomeric myosin VI, which are nonprocessive in single molecule assays, can coordinate to transport cargo with similar speeds as dimers.
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What OpenQuestion holds
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.