ArticleMolecular biology of the cell2001
Amino acid substitutions of coiled-coil protein Tpr abrogate anchorage to the nuclear pore complex but not parallel, in-register homodimerization.
Article in Molecular biology of the cell, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed, 61 citations in OpenAlex.
- Mlp1 and Mlp2 cooperate to build a stoichiometric nuclear pore basket in budding yeast.Journal of cell science · 2026Article
- Nucleoporin TPR integrates MAPK signaling with mitogen-induced transcriptional programs.Cell death & disease · 2026Article
- Advances in the understanding of nuclear pore complexes in human diseases.Journal of cancer research and clinical oncology · 2024Review
- TPR is a prognostic biomarker and potential therapeutic target associated with immune infiltration in hepatocellular carcinoma.Molecular and clinical oncology · 2024Article
- Fission yeast essential nuclear pore protein Nup211 regulates the expression of genes involved in cytokinesis.PloS one · 2024Article
- An evolutionarily conserved bimodular domain anchors ZC3HC1 and its yeast homologue Pml39p to the nuclear basket.Molecular biology of the cell · 2023Article
- ZC3HC1 is a structural element of the nuclear basket effecting interlinkage of TPR polypeptides.Molecular biology of the cell · 2022Article
- Pathogenic variants in nucleoporin TPR (translocated promoter region, nuclear basket protein) cause severe intellectual disability in humans.Human molecular genetics · 2022Article
- The 8p11 myeloproliferative syndrome: Genotypic and phenotypic classification and targeted therapy.Frontiers in oncology · 2022Review
- Article
- The human nucleoporin Tpr protects cells from RNA-mediated replication stress.Nature communications · 2021Article
- Tpr Deficiency Disrupts Erythroid Maturation With Impaired Chromatin Condensation in Zebrafish Embryogenesis.Frontiers in cell and developmental biology · 2021Article
- The Structure of the Nuclear Pore Complex (An Update).Annual review of biochemistry · 2019Review
- Tpr regulates the total number of nuclear pore complexes per cell nucleus.Genes & development · 2018Article
- Mitotic Disassembly of Nuclear Pore Complexes Involves CDK1- and PLK1-Mediated Phosphorylation of Key Interconnecting Nucleoporins.Developmental cell · 2017Article
- Activity of fibroblast growth factor receptor inhibitors TKI258, ponatinib and AZD4547 against TPR‑FGFR1 fusion.Molecular medicine reports · 2017Article
- Structural Study of MPN387, an Essential Protein for Gliding Motility of a Human-Pathogenic Bacterium, Mycoplasma pneumoniae.Journal of bacteriology · 2016Article
- The interaction of CRM1 and the nuclear pore protein Tpr.PloS one · 2014Article
- Structural characterization of altered nucleoporin Nup153 expression in human cells by thin-section electron microscopy.Nucleus (Austin, Tex.) · 2014Article
- The nuclear basket proteins Mlp1p and Mlp2p are part of a dynamic interactome including Esc1p and the proteasome.Molecular biology of the cell · 2013Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Tpr is a protein component of nuclear pore complex (NPC)-attached intranuclear filaments. Secondary structure predictions suggest a bipartite structure, with a large N-terminal domain dominated by heptad repeats (HRs) typical for coiled-coil--forming proteins. Proposed functions for Tpr have included roles as a homo- or heteropolymeric architectural element of the nuclear interior. To gain insight into Tpr's ultrastructural properties, we have studied recombinant Tpr segments by circular dichroism spectroscopy, chemical cross-linking, and rotary shadowing electron microscopy. We show that polypeptides of the N-terminal domain homodimerize in vitro and represent alpha-helical molecules of extended rod-like shape. With the use of a yeast two-hybrid approach, arrangement of the coiled-coil is found to be in parallel and in register. To clarify whether Tpr can self-assemble further into homopolymeric filaments, the full-length protein and deletion mutants were overexpressed in human cells and then analyzed by confocal immunofluorescence microscopy, cell fractionation, and immuno-electron microscopy. Surplus Tpr, which does not bind to the NPC, remains in a soluble state of approximately 7.5 S and occasionally forms aggregates of entangled molecules but neither self-assembles into extended linear filaments nor stably binds to other intranuclear structures. Binding to the NPC is shown to depend on the integrity of individual HRs; amino acid substitutions within these HRs abrogate NPC binding and render the protein soluble but do not abolish Tpr's general ability to homodimerize. Possible contributions of Tpr to the structural organization of the nuclear periphery in somatic cells are discussed.
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