ArticleRNA (New York, N.Y.)2009
Formation of She2p tetramers is required for mRNA binding, mRNP assembly, and localization.
Article in RNA (New York, N.Y.), 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 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
27 citing papers in PubMed, 44 citations in OpenAlex.
- Intrinsically disordered RNA-binding motifs cooperate to catalyze RNA folding and drive phase separation.Nucleic acids research · 2024Article
- Phosphorylation controls the oligomeric state of She2 and mRNA localization in yeast.RNA (New York, N.Y.) · 2023Article
- Molecular architecture and dynamics of ASH1 mRNA recognition by its mRNA-transport complex.Nature structural & molecular biology · 2017Article
- Hooking She3p onto She2p for myosin-mediated cytoplasmic mRNA transport.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- ASH1 mRNP-core factors form stable complexes in absence of cargo RNA at physiological conditions.RNA biology · 2015Article
- The novel proteins Rng8 and Rng9 regulate the myosin-V Myo51 during fission yeast cytokinesis.The Journal of cell biology · 2014Article
- Structural insights into the assembly of a monomeric class V myosin.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Structure of a myosin•adaptor complex and pairing by cargo.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Of social molecules: The interactive assembly of ASH1 mRNA-transport complexes in yeast.RNA biology · 2014Review
- A single molecule approach to mRNA transport by a class V myosin.RNA biology · 2014Article
- Here, there, everywhere. mRNA localization in budding yeast.RNA biology · 2014Review
- Role of Loc1p in assembly and reorganization of nuclear ASH1 messenger ribonucleoprotein particles in yeast.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- In vitro reconstitution of an mRNA-transport complex reveals mechanisms of assembly and motor activation.The Journal of cell biology · 2013Article
- Association of the yeast RNA-binding protein She2p with the tubular endoplasmic reticulum depends on membrane curvature.The Journal of biological chemistry · 2013Article
- Purification, crystallization and preliminary crystallographic analysis of the globular domain of the human type V myosin Myo5a.Acta crystallographica. Section F, Structural biology and crystallization communications · 2013Article
- Structural insights into the globular tails of the human type v myosins Myo5a, Myo5b, And Myo5c.PloS one · 2013Article
- Principles of mRNA transport in yeast.Cellular and molecular life sciences : CMLS · 2012Review
- Assembly of mRNA-protein complexes for directional mRNA transport in eukaryotes--an overview.Current protein & peptide science · 2012Review
- Transient CPEB dimerization and translational control.RNA (New York, N.Y.) · 2012Article
- Control of cytoplasmic mRNA localization.Cellular and molecular life sciences : CMLS · 2012Review
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In eukaryotic cells, dozens to hundreds of different mRNAs are localized by specialized motor-dependent transport complexes. One of the best-studied examples for directional mRNA transport is the localization of ASH1 mRNA in Saccharomyces cerevisiae. For transport, ASH1 mRNA is bound by the unusual RNA-binding protein She2p. Although previous results indicated that She2p forms dimers required for RNA binding and transcript localization, it remained unclear if the dimer constitutes the minimal RNA-binding unit assembling in vivo. By using analytical ultracentrifugation we found that She2p forms larger oligomeric complexes in solution. We also identified a point mutant that shows impaired oligomer formation. Size-exclusion chromatography suggests that She2p forms defined tetramers at physiological concentrations. Subsequent structural studies by small-angle X-ray scattering confirmed this finding and demonstrated that the previously observed She2p dimers interact in a head-to-head conformation to form an elongated tetrameric complex. This She2p tetramer suggests the generation of large continuous RNA-binding surfaces at both sides of the complex. Biochemical studies and immunostaining of cells confirmed that She2p tetramer formation is required for RNA binding, efficient mRNP assembly, and mRNA localization in vivo. Our finding on She2p tetramerization resolves previously raised questions on complex formation and mRNP function.
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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.