ArticleProceedings of the National Academy of Sciences of the United States of America2013
Role of Loc1p in assembly and reorganization of nuclear ASH1 messenger ribonucleoprotein particles in yeast.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed.
- Intrinsically disordered RNA-binding motifs cooperate to catalyze RNA folding and drive phase separation.Nucleic acids research · 2024Article
- Deciphering the RNA-binding protein network during endosomal mRNA transport.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Phosphorylation controls the oligomeric state of She2 and mRNA localization in yeast.RNA (New York, N.Y.) · 2023Article
- Linking transport and translation of mRNAs with endosomes and mitochondria.EMBO reports · 2021Review
- mRNA Localization in Plant Cells.Plant physiology · 2020Review
- Characterization of the Methanomicrobial Archaeal RNase Zs for Processing the CCA-Containing tRNA Precursors.Frontiers in microbiology · 2020Article
- Functional association of Loc1 and Puf6 with RNA helicase Dhh1 in translational regulation of Saccharomyces cerevisiae Ste12.PloS one · 2019Article
- Ribosome Biogenesis Modulates Ty1 Copy Number Control inGenetics · 2017Article
- Molecular architecture and dynamics of ASH1 mRNA recognition by its mRNA-transport complex.Nature structural & molecular biology · 2017Article
- The Roles of Puf6 and Loc1 in 60S Biogenesis Are Interdependent, and Both Are Required for Efficient Accommodation of Rpl43.The Journal of biological chemistry · 2016Article
- Conserved RNA-binding proteins required for dendrite morphogenesis in Caenorhabditis elegans sensory neurons.G3 (Bethesda, Md.) · 2015Article
- 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
- A divergent Pumilio repeat protein family for pre-rRNA processing and mRNA localization.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Co-transcriptional recruitment of Puf6 by She2 couples translational repression to mRNA localization.Nucleic acids research · 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
- Here, there, everywhere. mRNA localization in budding yeast.RNA biology · 2014Review
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5 authors.
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No grant is acknowledged in the PubMed record.
Abstract
Directional transport of mRNA is a universal feature in eukaryotes, requiring the assembly of motor-dependent RNA-transport particles. The cytoplasmic transport of mRNAs is preceded by the nuclear assembly of pre-messenger ribonucleoprotein particles (mRNPs). In budding yeast, the asymmetric synthesis of HO 1 (ASH1) pre-mRNP originates already cotranscriptionally and passes through the nucleolus before its nuclear export. The nucleolar localization of ASH1 mRNA protein 1 (Loc1p) is required for efficient ASH1 mRNA localization. Immunoprecipitation experiments have revealed that Loc1p forms cocomplexes with other components of the ASH1 transport complex. However, it remains unclear how Loc1p is recruited into this mRNP and why Loc1p is important for ASH1 mRNA localization. Here we demonstrate that Loc1p undergoes a direct and specific interaction with the ASH1 mRNA-binding Swi5p-dependent HO expression protein 2 (She2p). This cocomplex shows higher affinity and specificity for RNA bearing localization elements than the individual proteins. It also stabilizes the otherwise transient binding of She2p to ASH1 mRNA, suggesting that cooperative mRNA binding of Loc1p with She2p is the required nuclear function of Loc1p for ASH1 mRNA localization. After nuclear export, myosin-bound She3p joins the ASH1 mRNP to form a highly specific cocomplex with She2p and ASH1 mRNA. Because Loc1p is found only in the nucleus, it must be removed from the complex directly before or after export. In vitro and in vivo experiments indicate that the synergistic interaction of She2p and She3p displaces Loc1p from the ASH1 complex, allowing free Loc1p to rapidly reenter the nucle(ol)us. Together these findings suggest an ordered process of nuclear assembly and reorganization for the maturation of localizing ASH1 mRNPs.
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