ArticleThe Journal of biological chemistry2010
Control of mRNA export and translation termination by inositol hexakisphosphate requires specific interaction with Gle1.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.
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Who cites it
58 citing papers in PubMed.
- Arabidopsis inositol polyphosphate kinase activities regulate COP9 deneddylation functions in phosphate homeostasis.Journal of integrative plant biology · 2026Article
- From Obscurity to Prominence: IPMK's Expanding Role in Cellular Signaling, Physiology, and Disease.Biomolecules · 2025Review
- Identification of divergentbioRxiv : the preprint server for biology · 2025Article
- Molecular Structure of the mRNA Export Factor Gle1 fromInternational journal of molecular sciences · 2025Article
- Advances in the understanding of nuclear pore complexes in human diseases.Journal of cancer research and clinical oncology · 2024Review
- Spelling out the roles of individual nucleoporins in nuclear export of mRNA.Nucleus (Austin, Tex.) · 2022Review
- Features and factors that dictate if terminating ribosomes cause or counteract nonsense-mediated mRNA decay.The Journal of biological chemistry · 2022Review
- Unraveling docking and initiation of mRNA export through the nuclear pore complex.BioEssays : news and reviews in molecular, cellular and developmental biology · 2022Article
- The nucleoporin Gle1 activates DEAD-box protein 5 (Dbp5) by promoting ATP binding and accelerating rate limiting phosphate release.Nucleic acids research · 2022Article
- Distinct roles of nuclear basket proteins in directing the passage of mRNA through the nuclear pore.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Nuclear mRNA maturation and mRNA export control: from trypanosomes to opisthokonts.Parasitology · 2021Review
- Emerging molecular functions and novel roles for the DEAD-box protein Dbp5/DDX19 in gene expression.Cellular and molecular life sciences : CMLS · 2021Review
- Mutation Screening of theFrontiers in neuroscience · 2021Article
- Pharmacological approaches for targeting cystic fibrosis nonsense mutations.European journal of medicinal chemistry · 2020Review
- Extension of the phenotypic spectrum of GLE1-related disorders to a mild congenital form resembling congenital myopathy.Molecular genetics & genomic medicine · 2020Article
- Dbp5/DDX19 between Translational Readthrough and Nonsense Mediated Decay.International journal of molecular sciences · 2020Review
- Article
- Translation termination depends on the sequential ribosomal entry of eRF1 and eRF3.Nucleic acids research · 2019Article
- Fungal Kinases With a Sweet Tooth: Pleiotropic Roles of Their Phosphorylated Inositol Sugar Products in the Pathogenicity ofFrontiers in cellular and infection microbiology · 2019Review
- Nup159 Weakens Gle1 Binding to Dbp5 But Does Not Accelerate ADP Release.Journal of molecular biology · 2018Article
Corrections and comments
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Authors and funding
3 authors.
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Abstract
The unidirectional translocation of messenger RNA (mRNA) through the aqueous channel of the nuclear pore complex (NPC) is mediated by interactions between soluble mRNA export factors and distinct binding sites on the NPC. At the cytoplasmic side of the NPC, the conserved mRNA export factors Gle1 and inositol hexakisphosphate (IP(6)) play an essential role in mRNA export by activating the ATPase activity of the DEAD-box protein Dbp5, promoting localized messenger ribonucleoprotein complex remodeling, and ensuring the directionality of the export process. In addition, Dbp5, Gle1, and IP(6) are also required for proper translation termination. However, the specificity of the IP(6)-Gle1 interaction in vivo is unknown. Here, we characterize the biochemical interaction between Gle1 and IP(6) and the relationship to Dbp5 binding and stimulation. We identify Gle1 residues required for IP(6) binding and show that these residues are needed for IP(6)-dependent Dbp5 stimulation in vitro. Furthermore, we demonstrate that Gle1 is the primary target of IP(6) for both mRNA export and translation termination in vivo. In Saccharomyces cerevisiae cells, the IP(6)-binding mutants recapitulate all of the mRNA export and translation termination defects found in mutants depleted of IP(6). We conclude that Gle1 specifically binds IP(6) and that this interaction is required for the full potentiation of Dbp5 ATPase activity during both mRNA export and translation termination.
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