ArticlePloS one2011
Myosin VI regulates actin structure specialization through conserved cargo-binding domain sites.
Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 20 citations in OpenAlex.
- Actin from within - how nuclear myosins and actin regulate nuclear architecture and mechanics.Journal of cell science · 2025Review
- Myosin VI is expressed in developing ovarian follicles inFrontiers in cell and developmental biology · 2025Article
- PFTAIRE Kinase L63 Interactor 1A (Pif1A Protein) Is Required for Actin Cone Movement during Spermatid Individualization inInternational journal of molecular sciences · 2022Article
- Diverse functions of myosin VI in spermiogenesis.Histochemistry and cell biology · 2021Review
- Loss of myosin VI expression affects acrosome/acroplaxome complex morphology during mouse spermiogenesis†.Biology of reproduction · 2020Article
- Myosin VI maintains the actin-dependent organization of the tubulobulbar complexes required for endocytosis during mouse spermiogenesis†‡.Biology of reproduction · 2020Article
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- Distinct roles of two myosins in C. elegans spermatid differentiation.PLoS biology · 2019Article
- Disruption ofG3 (Bethesda, Md.) · 2018Article
- Expression and localization of myosin VI in developing mouse spermatids.Histochemistry and cell biology · 2017Article
- Drosophila LKB1 is required for the assembly of the polarized actin structure that allows spermatid individualization.PloS one · 2017Article
- miR-8 modulates cytoskeletal regulators to influence cell survival and epithelial organization in Drosophila wings.Developmental biology · 2016Article
- Separating from the pack: Molecular mechanisms ofSpermatogenesisArticle
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 3 countries.
Funding
Abstract
Actin structures are often stable, remaining unchanged in organization for the lifetime of a differentiated cell. Little is known about stable actin structure formation, organization, or maintenance. During Drosophila spermatid individualization, long-lived actin cones mediate cellular remodeling. Myosin VI is necessary for building the dense meshwork at the cones' fronts. We test several ideas for myosin VI's mechanism of action using domain deletions or site-specific mutations of myosin VI. The head (motor) and globular tail (cargo-binding) domains were both needed for localization at the cone front and dense meshwork formation. Several conserved partner-binding sites in the globular tail previously identified in vertebrate myosin VI were critical for function in cones. Localization and promotion of proper actin organization were separable properties of myosin VI. A vertebrate myosin VI was able to localize and function, indicating that functional properties are conserved. Our data eliminate several models for myosin VI's mechanism of action and suggest its role is controlling organization and action of actin assembly regulators through interactions at conserved sites. The Drosophila orthologues of interaction partners previously identified for vertebrate myosin VI are likely not required, indicating novel partners mediate this effect. These data demonstrate that generating an organized and functional actin structure in this cell requires multiple activities coordinated by myosin VI.
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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.