ArticleMolecular biology of the cell2006
Mutations in tap uncouple RNA export activity from translocation through the nuclear pore complex.
Article in Molecular biology of the cell, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 24 citations in OpenAlex.
- Novel nuclear RNA export factor 1 adaptor drives tumor growth by increasing proliferation-stimulatory mRNA export.Signal transduction and targeted therapy · 2026Article
- Porcine Reproductive and Respiratory Syndrome Virus Nonstructural Protein 1 Beta Interacts with Nucleoporin 62 To Promote Viral Replication and Immune Evasion.Journal of virology · 2019Article
- Export of piRNA precursors by EJC triggers assembly of cytoplasmic Yb-body in Drosophila.Nature communications · 2016Article
- RanBP2/Nup358 potentiates the translation of a subset of mRNAs encoding secretory proteins.PLoS biology · 2013Article
- Localization of nucleoporin Tpr to the nuclear pore complex is essential for Tpr mediated regulation of the export of unspliced RNA.PloS one · 2012Article
- Nucleo-cytoplasmic transport of proteins and RNA in plants.Plant cell reports · 2011Review
- ATP is required for interactions between UAP56 and two conserved mRNA export proteins, Aly and CIP29, to assemble the TREX complex.Genes & development · 2010Article
- The Arabidopsis nuclear pore and nuclear envelope.The arabidopsis book · 2010Article
- Fragile X mental retardation protein FMRP binds mRNAs in the nucleus.Molecular and cellular biology · 2009Article
- Centrin 2 localizes to the vertebrate nuclear pore and plays a role in mRNA and protein export.Molecular and cellular biology · 2008Article
- Formation of a Tap/NXF1 homotypic complex is mediated through the amino-terminal domain of Tap and enhances interaction with nucleoporins.Molecular biology of the cell · 2008Article
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
Interactions between transport receptors and phenylalanine-glycine (FG) repeats on nucleoporins drive the translocation of receptor-cargo complexes through nuclear pores. Tap, a transport receptor that mediates nuclear export of cellular mRNAs, contains a UBA-like and NTF2-like folds that can associate directly with FG repeats. In addition, two nuclear export sequences (NESs) within the NTF2-like region can also interact with nucleoporins. The Tap-RNA complex was shown to bind to three nucleoporins, Nup98, p62, and RanBP2, and these interactions were enhanced by Nxt1. Mutations in the Tap-UBA region abolished interactions with all three nucleoporins, whereas the effect of point mutations within the NTF2-like domain of Tap known to disrupt Nxt1 binding or nucleoporin binding were nucleoporin dependent. A mutation in any of these Tap domains was sufficient to reduce RNA export but was not sufficient to disrupt Tap interaction with the NPC in vivo or its nucleocytoplasmic shuttling. However, shuttling activity was reduced or abolished by combined mutations within the UBA and either the Nxt1-binding domain or NESs. These data suggest that Tap requires both the UBA- and NTF2-like domains to mediate the export of RNA cargo, but can move through the pores independently of these domains when free of RNA cargo.
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