ArticleThe Journal of biological chemistry2011
Myosin Va is required for P body but not stress granule formation.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 20 citations in OpenAlex.
- Actin-dependent recruitment of AGO2 to the zonula adherens.Molecular biology of the cell · 2023Article
- Myosin 5a in the Urinary Bladder: Localization, Splice Variant Expression, and Functional Role in Neurotransmission.Frontiers in physiology · 2022Article
- Complex Interactions Between Membrane-Bound Organelles, Biomolecular Condensates and the Cytoskeleton.Frontiers in cell and developmental biology · 2020Review
- Mammalian microtubule P-body dynamics are mediated by nesprin-1.The Journal of cell biology · 2014Article
- Processing-body movement in Arabidopsis depends on an interaction between myosins and DECAPPING PROTEIN1.Plant physiology · 2014Article
- Composition and function of P bodies in Arabidopsis thaliana.Frontiers in plant science · 2014Review
- Myrip couples the capture of secretory granules by the actin-rich cell cortex and their attachment to the plasma membrane.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2012Article
- Unraveling regulation and new components of human P-bodies through a protein interaction framework and experimental validation.RNA (New York, N.Y.) · 2011Article
- Stress granule and P-body clearance: Seeking coherence in acts of disappearance.Seminars in cell & developmental biologyReview
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In the present study we demonstrate an association between mammalian myosin Va and cytoplasmic P bodies, microscopic ribonucleoprotein granules that contain components of the 5'-3' mRNA degradation machinery. Myosin Va colocalizes with several P body markers and its RNAi-mediated knockdown results in the disassembly of P bodies. Overexpression of a dominant-negative mutant of myosin Va reduced the motility of P bodies in living cells. Co-immunoprecipitation experiments demonstrate that myosin Va physically associates with eIF4E, an mRNA binding protein that localizes to P bodies. In contrast, we find that myosin Va does not play a role in stress granule formation. Stress granules are ribonucleoprotein structures that are involved in translational silencing and are spatially, functionally, and compositionally linked to P bodies. Myosin Va is found adjacent to stress granules in stressed cells but displays minimal localization within stress granules, and myosin Va knockdown has no effect on stress granule assembly or disassembly. Combined with recently published reports demonstrating a role for Drosophila and mammalian class V myosins in mRNA transport and the involvement of the yeast myosin V orthologue Myo2p in P body assembly, our results provide further evidence that the class V myosins serve an important role in the transport and turnover of mRNA.
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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.