ArticleJournal of cell science2014
Phosphorylation of nucleoporin Tpr governs its differential localization and is required for its mitotic function.
Article in Journal of cell science, 2014. 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 19 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
19 citing papers in PubMed, 35 citations in OpenAlex.
- TPR is required for circRNA, lncRNA and mRNA nuclear export.Non-coding RNA research · 2026Article
- 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
- Structure, Maintenance, and Regulation of Nuclear Pore Complexes: The Gatekeepers of the Eukaryotic Genome.Cold Spring Harbor perspectives in biology · 2022Review
- Phosphoproteomic characterization of the signaling network resulting from activation of the chemokine receptor CCR2.The Journal of biological chemistry · 2020Article
- The Quest for the Blueprint of the Nuclear Pore Complex.The protein journal · 2019Review
- Nuclear pore protein TPR associates with lamin B1 and affects nuclear lamina organization and nuclear pore distribution.Cellular and molecular life sciences : CMLS · 2019Article
- Article
- Tpr regulates the total number of nuclear pore complexes per cell nucleus.Genes & development · 2018Article
- Delineating FtsQ-mediated regulation of cell division inThe Journal of biological chemistry · 2018Article
- Colorectal cancer cells require glycogen synthase kinase-3β for sustaining mitosis via translocated promoter region (TPR)-dynein interaction.Oncotarget · 2018Article
- The fission yeast nucleoporin Alm1 is required for proteasomal degradation of kinetochore components.The Journal of cell biology · 2017Article
- Nucleoporins redistribute inside the nucleus after cell cycle arrest induced by histone deacetylases inhibition.Nucleus (Austin, Tex.) · 2017Article
- Structural Basis of TPR-Mediated Oligomerization and Activation of Oncogenic Fusion Kinases.Structure (London, England : 1993) · 2017Article
- AKAP95 interacts with nucleoporin TPR in mitosis and is important for the spindle assembly checkpoint.Cell cycle (Georgetown, Tex.) · 2017Article
- Time-resolved Phosphoproteome Analysis of Paradoxical RAF Activation Reveals Novel Targets of ERK.Molecular & cellular proteomics : MCP · 2017Article
- Review
- Nuclear pore proteins and the control of genome functions.Genes & development · 2015Review
- Review
Corrections and comments
- Erratum issued
Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
A major constituent of the nuclear basket region of the nuclear pore complex (NPC), nucleoporin Tpr, plays roles in regulating multiple important processes. We have previously established that Tpr is phosphorylated in both a MAP-kinase-dependent and MAP-kinase-independent manner, and that Tpr acts as both a substrate and as a scaffold for ERK2 (also known as MAPK1). Here, we report the identification of S2059 and S2094 as the major novel ERK-independent phosphorylation sites and T1677, S2020, S2023 and S2034 as additional ERK-independent phosphorylation sites found in the Tpr protein in vivo. Our results suggest that protein kinase A phosphorylates the S2094 residue and that the site is hyperphosphorylated during mitosis. Furthermore, we find that Tpr is phosphorylated at the S2059 residue by CDK1 and the phosphorylated form distinctly localizes with chromatin during telophase. Abrogation of S2059 phosphorylation abolishes the interaction of Tpr with Mad1, thus compromising the localization of both Mad1 and Mad2 proteins, resulting in cell cycle defects. The identification of novel phosphorylation sites on Tpr and the observations presented in this study allow better understanding of Tpr functions.
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Registered trials
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.