ArticleBMC cell biology2009
Karyopherin binding interactions and nuclear import mechanism of nuclear pore complex protein Tpr.
Article in BMC cell biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 38 citations in OpenAlex.
- Hydrophobic interactions of FG-nucleoporins are required for dilating nuclear membrane pores into selective transport channels after mitosis.Nature structural & molecular biology · 2026Article
- Viral interference of nucleocytoplasmic transport.The Journal of biological chemistry · 2025Review
- Hydrophobic interactions of FG-nucleoporins are required for dilating nuclear membrane pores into selective transport channels after mitosis.bioRxiv : the preprint server for biology · 2025Article
- The Potential of Nuclear Pore Complexes in Cancer Therapy.Molecules (Basel, Switzerland) · 2024Review
- Spelling out the roles of individual nucleoporins in nuclear export of mRNA.Nucleus (Austin, Tex.) · 2022Review
- Unraveling docking and initiation of mRNA export through the nuclear pore complex.BioEssays : news and reviews in molecular, cellular and developmental biology · 2022Article
- Long noncoding RNA TLNC1 promotes the growth and metastasis of liver cancer via inhibition of p53 signaling.Molecular cancer · 2022Article
- The 8p11 myeloproliferative syndrome: Genotypic and phenotypic classification and targeted therapy.Frontiers in oncology · 2022Review
- Super-resolved 3D tracking of cargo transport through nuclear pore complexes.Nature cell biology · 2022Article
- Nucleoporin TPR promotes tRNA nuclear export and protein synthesis in lung cancer cells.PLoS genetics · 2021Article
- Confinement hinders motility by inducing RhoA-mediated nuclear influx, volume expansion, and blebbing.The Journal of cell biology · 2019Article
- Nup2 performs diverse interphase functions in Aspergillus nidulans.Molecular biology of the cell · 2018Article
- Article
- Orchestrating the Selection and Packaging of Genomic RNA by Retroviruses: An Ensemble of Viral and Host Factors.Viruses · 2016Review
- Transportin acts to regulate mitotic assembly events by target binding rather than Ran sequestration.Molecular biology of the cell · 2014Article
- The interaction of CRM1 and the nuclear pore protein Tpr.PloS one · 2014Article
- Defective nuclear import of Tpr in Progeria reflects the Ran sensitivity of large cargo transport.The Journal of cell biology · 2013Article
- The huntingtin N17 domain is a multifunctional CRM1 and Ran-dependent nuclear and cilial export signal.Human molecular genetics · 2013Article
- An N-terminal nuclear export signal regulates trafficking and aggregation of Huntingtin (Htt) protein exon 1.The Journal of biological chemistry · 2013Article
- Regulation of nucleocytoplasmic trafficking of viral proteins: an integral role in pathogenesis?Biochimica et biophysica acta · 2011Review
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
backgroundTpr is a large protein with an extended coiled-coil domain that is localized within the nuclear basket of the nuclear pore complex. Previous studies 1 involving antibody microinjection into mammalian cells suggested a role for Tpr in nuclear export of proteins via the CRM1 export receptor. In addition, Tpr was found to co-immunoprecipitate with importins alpha and beta from Xenopus laevis egg extracts 2, although the function of this is unresolved. Yeast Mlp1p and Mlp2p, which are homologous to vertebrate Tpr, have been implicated in mRNA surveillance to retain unspliced mRNAs in the nucleus34. To augment an understanding of the role of Tpr in nucleocytoplasmic trafficking, we explored the interactions of recombinant Tpr with the karyopherins CRM1, importin beta and importin alpha by solid phase binding assays. We also investigated the conditions required for nuclear import of Tpr using an in vitro assay.
resultsWe found that Tpr binds strongly and specifically to importin alpha, importin beta, and a CRM1 containing trimeric export complex, and that the binding sites for importins alpha and beta are distinct. We also determined that the nuclear import of Tpr is dependent on cytosolic factors and energy and is efficiently mediated by the importin alpha/beta import pathway.
conclusionBased on the binding and nuclear import assays, we propose that Tpr is imported into the nucleus by the importin alpha/beta heterodimer. In addition, we suggest that Tpr can serve as a nucleoporin binding site for importin beta during import of importin beta cargo complexes and/or importin beta recycling. Our finding that Tpr bound preferentially to CRM1 in an export complex strengthens the notion that Tpr is involved in protein export.
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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.