ArticleJournal of molecular biology2012
The structure of the NXF2/NXT1 heterodimeric complex reveals the combined specificity and versatility of the NTF2-like fold.
Article in Journal of molecular biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 23 citations in OpenAlex.
- Division of labor in trypanosome RNA processing and export through expanded Mex67 paralogs.Nucleic acids research · 2026Article
- Unveiling the dynamics and therapeutic potential of mInternational journal of biological sciences · 2025Review
- Nuclear transport proteins: structure, function, and disease relevance.Signal transduction and targeted therapy · 2023Review
- Sending the message: specialized RNA export mechanisms in trypanosomes.Trends in parasitology · 2022Review
- Piwi-piRNA complexes induce stepwise changes in nuclear architecture at target loci.The EMBO journal · 2021Article
- A Pandas complex adapted for piRNA-guided transcriptional silencing and heterochromatin formation.Nature cell biology · 2019Article
- Nuclear RNA export factor variant initiates piRNA-guided co-transcriptional silencing.The EMBO journal · 2019Article
- Reduction of mRNA export unmasks different tissue sensitivities to low mRNA levels during Caenorhabditis elegans development.PLoS genetics · 2019Article
- Article
- Integration of mRNP formation and export.Cellular and molecular life sciences : CMLS · 2017Review
- Structural characterization of the principal mRNA-export factor Mex67-Mtr2 from Chaetomium thermophilum.Acta crystallographica. Section F, Structural biology communications · 2015Article
- Domain organization within the nuclear export factor Mex67:Mtr2 generates an extended mRNA binding surface.Nucleic acids research · 2015Article
- A specific set of exon junction complex subunits is required for the nuclear retention of unspliced RNAs in Caenorhabditis elegans.Molecular and cellular biology · 2013Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
NXF1-like members of the NXF (nuclear export factor) family orchestrate bulk nuclear export of mRNA, while functionally distinct NXF variant proteins carry out separate substrate-specific and tissue-specific RNA regulation. Metazoan organisms possess at least one NXF1-like gene and one or more NXF variant genes. Heterodimerization of both proteins with the NXT (NTF2-related export) protein is central to NXF family function; however, given the multiplicity of NXF/NXT complexes, the specificity and mechanism of heterodimerization remain unclear. Here, we report the structural and functional analyses of the Caenorhabditis elegans NXF variant ceNXF2 bound to ceNXT1. Contacts crucial for NXF/NXT heterodimer stability and specificity, including a probable site for phosphoregulation, have been identified. The ceNXF2 NTF2 domain bears at least two nucleoporin (Nup) binding pockets necessary for the colocalization of ceNXF2/ceNXT1 at the nuclear envelope. Unexpectedly, one Nup binding pocket is formed at the heterodimer interface of the ceNXF2/ceNXT1 complex, demonstrating that NXT binding directly regulates NXF function.
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