ArticleMolecular biology of the cell2003
Direct interaction with nup153 mediates binding of Tpr to the periphery of the nuclear pore complex.
Article in Molecular biology of the cell, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 119 papers.
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Who cites it
119 citing papers in PubMed, 184 citations in OpenAlex.
- Nucleoporins in Cancer: Functional Roles and Therapeutic Opportunities.Cancer discovery · 2026Article
- Progerin-induced nuclear envelope remodeling is shaped by cell division and NUP153.Journal of cell science · 2026Article
- Nucleoporin TPR integrates MAPK signaling with mitogen-induced transcriptional programs.Cell death & disease · 2026Article
- Structure, function and assembly of nuclear pore complexes.Nature reviews. Molecular cell biology · 2026Review
- Viral interference of nucleocytoplasmic transport.The Journal of biological chemistry · 2025Review
- Nup153 and TPR/Megator Interact with TREX-2 Subunits and Are Essential for TREX-2-Dependent Nuclear Export ofInternational journal of molecular sciences · 2025Article
- An interkinetic envelope surrounds chromosomes between meiosis I and II in C. elegans oocytes.The Journal of cell biology · 2025Article
- ZC3HC1 has many functions distinct from TPR and is dispensable for TPR localisation to the nuclear basket.Wellcome open research · 2025Article
- Article
- Nuclear basket proteins regulate the distribution and mobility of nuclear pore complexes in budding yeast.Molecular biology of the cell · 2024Article
- An interkinetic envelope surrounds chromosomes between meiosis I and II inbioRxiv : the preprint server for biology · 2024Article
- Docking a flexible basket onto the core of the nuclear pore complex.Nature cell biology · 2024Article
- Advances in the understanding of nuclear pore complexes in human diseases.Journal of cancer research and clinical oncology · 2024Review
- Fission yeast essential nuclear pore protein Nup211 regulates the expression of genes involved in cytokinesis.PloS one · 2024Article
- Tpr Misregulation in Hippocampal Neural Stem Cells in Mouse Models of Alzheimer's Disease.Cells · 2023Article
- Mechanisms of nuclear pore complex disassembly by the mitotic Polo-like kinase 1 (PLK-1) inScience advances · 2023Article
- An evolutionarily conserved bimodular domain anchors ZC3HC1 and its yeast homologue Pml39p to the nuclear basket.Molecular biology of the cell · 2023Article
- Spelling out the roles of individual nucleoporins in nuclear export of mRNA.Nucleus (Austin, Tex.) · 2022Review
- A role for Nup153 in nuclear assembly reveals differential requirements for targeting of nuclear envelope constituents.Molecular biology of the cell · 2022Article
- Nup50 plays more than one instrument.Cell cycle (Georgetown, Tex.) · 2022Article
59 more citing papers are in PubMed but not listed here.
Corrections and comments
- Erratum issued
Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Tpr is a 267-kDa protein forming coiled coil-dominated homodimers that locate at the nucleoplasmic side of the nuclear pore complex (NPC). The proteins that tether Tpr to this location are unknown. Moreover, the question whether Tpr itself might act as a scaffold onto which other NPC components need to be assembled has not been answered to date. To assess Tpr's role as an architectural element of the NPC, we have studied the sequential disassembly and reassembly of NPCs in mitotic cells, paralleled by studies of cells depleted of Tpr as a result of posttranscriptional tpr gene silencing by RNA interference (RNAi). NPC assembly and recruitment of several nucleoporins, including Nup50, Nup93, Nup96, Nup98, Nup107, and Nup153, in anaphase/early telophase is shown to precede NPC association of Tpr in late telophase. In accordance, cellular depletion of Tpr by RNAi does not forestall binding of these nucleoporins to the NPC. In a search for proteins that moor Tpr to the NPC, we have combined the RNAi approach with affinity-chromatography and yeast two-hybrid interaction studies, leading to the identification of nucleoporin Nup153 as the binding partner for Tpr. The specificity of this interaction is demonstrated by its sensitivity to Tpr amino acid substitution mutations that abolish Tpr's ability to adhere to the NPC and affect the direct binding of Tpr to Nup153. Accordingly, cellular depletion of Nup153 by RNAi is shown to result in mislocalization of Tpr to the nuclear interior. Nup153 deficiency also causes mislocalization of Nup50 but has no direct effect on NPC localization of the other nucleoporins studied in this investigation. In summary, these results render Tpr a protein only peripherally attached to the NPC that does not act as an essential scaffold for other nucleoporins.
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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.