ArticleMolecular biology of the cell2008
Formation of a Tap/NXF1 homotypic complex is mediated through the amino-terminal domain of Tap and enhances interaction with nucleoporins.
Article in Molecular biology of the cell, 2008. 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, 17 citations in OpenAlex.
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- A Pandas complex adapted for piRNA-guided transcriptional silencing and heterochromatin formation.Nature cell biology · 2019Article
- An NXF1 mRNA with a retained intron is expressed in hippocampal and neocortical neurons and is translated into a protein that functions as an Nxf1 cofactor.Molecular biology of the cell · 2016Article
- Multiple Export Mechanisms for mRNAs.Cells · 2015Review
- Evolutionary conservation of a molecular machinery for export and expression of mRNAs with retained introns.RNA (New York, N.Y.) · 2015Article
- Review
- TREX exposes the RNA-binding domain of Nxf1 to enable mRNA export.Nature communications · 2012Article
- A brain-derived MeCP2 complex supports a role for MeCP2 in RNA processing.Bioscience reports · 2011Article
- Facioscapulohumeral muscular dystrophy region gene 1 is a dynamic RNA-associated and actin-bundling protein.Journal of molecular biology · 2011Article
- Facioscapulohumeral muscular dystrophy (FSHD) region gene 1 (FRG1) is a dynamic nuclear and sarcomeric protein.Differentiation; research in biological diversity · 2011Article
- Fragile X mental retardation protein FMRP binds mRNAs in the nucleus.Molecular and cellular biology · 2009Article
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3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Nuclear export of mRNAs is mediated by the Tap/Nxt1 pathway. Tap moves its RNA cargo through the nuclear pore complex by direct interaction with nucleoporin phenylalanine-glycine repeats. This interaction is strengthened by the formation of a Tap/Nxt1 heterodimer. We now present evidence that Tap can form a multimeric complex with itself and with other members of the NXF family. We also show that the homotypic Tap complex can interact with both Nxt1 and nucleoporins in vitro. The region mediating this oligomerization is localized to the first 187 amino acids of Tap, which overlaps with its RNA-binding domain. Removal of this domain greatly reduces the ability of Tap to bind nucleoporins in vitro and in vivo. This is the first report showing that the Tap amino terminus modulates the interaction of Tap with nucleoporins. We speculate that this mechanism has a regulatory role for RNA export independent of RNA binding.
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