ArticleThe EMBO journal2008
A versatile interaction platform on the Mex67-Mtr2 receptor creates an overlap between mRNA and ribosome export.
Article in The EMBO journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed, 58 citations in OpenAlex.
- Division of labor in trypanosome RNA processing and export through expanded Mex67 paralogs.Nucleic acids research · 2026Article
- Article
- Gle1 is required for tRNA to stimulate Dbp5 ATPase activitybioRxiv : the preprint server for biology · 2023Article
- Ribosome biogenesis factors-from names to functions.The EMBO journal · 2023Review
- Impact of inherent biases built into proteomic techniques: Proximity labeling and affinity capture compared.The Journal of biological chemistry · 2023Article
- Measuring and Interpreting Nuclear Transport in Neurodegenerative Disease-The Example of C9orf72 ALS.International journal of molecular sciences · 2021Review
- Emerging molecular functions and novel roles for the DEAD-box protein Dbp5/DDX19 in gene expression.Cellular and molecular life sciences : CMLS · 2021Review
- Article
- The Nuclear Export Receptors TbMex67 and TbMtr2 Are Required for Ribosome Biogenesis in Trypanosoma brucei.mSphere · 2019Article
- Placeholder factors in ribosome biogenesis: please, pave my way.Microbial cell (Graz, Austria) · 2017Review
- Ribosome-stalk biogenesis is coupled with recruitment of nuclear-export factor to the nascent 60S subunit.Nature structural & molecular biology · 2016Article
- Structural characterization of the principal mRNA-export factor Mex67-Mtr2 from Chaetomium thermophilum.Acta crystallographica. Section F, Structural biology communications · 2015Article
- NMD3 regulates both mRNA and rRNA nuclear export in African trypanosomes via an XPOI-linked pathway.Nucleic acids research · 2015Article
- Domain organization within the nuclear export factor Mex67:Mtr2 generates an extended mRNA binding surface.Nucleic acids research · 2015Article
- Article
- Review
- A RanGTP-independent mechanism allows ribosomal protein nuclear import for ribosome assembly.eLife · 2014Article
- The multifunctional nuclear pore complex: a platform for controlling gene expression.Current opinion in cell biology · 2014Review
- Ribosome biogenesis in the yeast Saccharomyces cerevisiae.Genetics · 2013Review
- Structure of the pre-60S ribosomal subunit with nuclear export factor Arx1 bound at the exit tunnel.Nature structural & molecular biology · 2012Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The transport receptor Mex67-Mtr2 functions in mRNA export, and also by a loop-confined surface on the heterodimer binds to and exports pre-60S particles. We show that Mex67-Mtr2 through the same surface that recruits pre-60S particles interacts with the Nup84 complex, a structural module of the nuclear pore complex devoid of Phe-Gly domains. In vitro, pre-60S particles and the Nup84 complex compete for an overlapping binding site on the loop-extended Mex67-Mtr2 surface. Chemical crosslinking identified Nup85 as the subunit in the Nup84 complex that directly binds to the Mex67 loop. Genetic studies revealed that this interaction is crucial for mRNA export. Notably, pre-60S subunit export impaired by mutating Mtr2 or the 60S adaptor Nmd3 could be partially restored by second-site mutation in Nup85 that caused dissociation of Mex67-Mtr2 from the Nup84 complex. Thus, the Mex67-Mtr2 export receptor employs a versatile binding platform on its surface that could create a crosstalk between mRNA and ribosome export pathways.
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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.