ArticleProceedings of the National Academy of Sciences of the United States of America2007
Cell-cycle-dependent phosphorylation of the nuclear pore Nup107-160 subcomplex.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.
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Who cites it
60 citing papers in PubMed, 95 citations in OpenAlex.
- CabioRxiv : the preprint server for biology · 2026Article
- Breaking barriers: Respiratory viral strategies targeting the host's nuclear pore complex and nuclear transport pathways.Molecular biology of the cell · 2026Review
- The role of phase separation for RNA and protein transport through the nuclear pore complex.Journal of experimental botany · 2026Review
- Structure, function and assembly of nuclear pore complexes.Nature reviews. Molecular cell biology · 2026Review
- Cytoplasmic nucleoporin assemblage: the cellular artwork in physiology and disease.Nucleus (Austin, Tex.) · 2024Review
- Crosstalk between mitotic reassembly and repair of the nuclear envelope.Nucleus (Austin, Tex.) · 2024Review
- Phosphorylation of ELYS promotes its interaction with VAPB at decondensing chromosomes during mitosis.EMBO reports · 2024Article
- Super-resolution microscopy reveals focal organization of ER-associated Y-complexes in mitosis.EMBO reports · 2023Article
- The role of inner nuclear membrane proteins in tumourigenesis and as potential targets for cancer therapy.Cancer metastasis reviews · 2022Review
- Maintaining Transcriptional Specificity Through Mitosis.Annual review of genomics and human genetics · 2022Review
- Cryo-EM structure of the inner ring from the Xenopus laevis nuclear pore complex.Cell research · 2022Article
- Structure, Maintenance, and Regulation of Nuclear Pore Complexes: The Gatekeepers of the Eukaryotic Genome.Cold Spring Harbor perspectives in biology · 2022Review
- Structural, enzymatic and spatiotemporal regulation of PP2A-B55 phosphatase in the control of mitosis.Frontiers in cell and developmental biology · 2022Review
- The LEM-ESCRT toolkit: Repair and maintenance of the nucleus.Frontiers in cell and developmental biology · 2022Review
- Analysis of Ubiquitylation and SUMOylation of Yeast Nuclear Pore Complex Proteins.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Epigenetic regulation of neural stem cells: The emerging role of nucleoporins.Stem cells (Dayton, Ohio) · 2021Review
- The Quest for the Blueprint of the Nuclear Pore Complex.The protein journal · 2019Review
- Phosphatases in Mitosis: Roles and Regulation.Biomolecules · 2019Review
- PP2A-B55 promotes nuclear envelope reformation after mitosis inThe Journal of cell biology · 2018Article
- Nucleoporin 107, 62 and 153 mediate Kcnq1ot1 imprinted domain regulation in extraembryonic endoderm stem cells.Nature communications · 2018Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
Abstract
The nuclear pore complex (NPC) mediates macromolecular transport between the nucleus and the cytoplasm. Many NPC proteins (nucleoporins, Nups) are modified by phosphorylation. It is believed that phosphorylation regulates the breakdown of the nuclear envelope at mitosis and the disassembly of the NPC into different subcomplexes. In this study, we examined the cell-cycle-dependent phosphorylation of the Nup107-160 subcomplex, a core building block of the NPC. Using in vivo (32)P labeling in HeLa cells, we found that Nup107, Nup96, and Nup133 are phosphorylated during mitosis. To precisely map the phosphorylation sites within the complex, we used a comprehensive multiple-stage MS approach (MS, MS(2), and MS(3)), establishing that Nup160, Nup133, Nup96, and Nup107 are all targets of phosphorylation. We determined that the phosphorylation sites are clustered mainly at the N-terminal regions of these proteins, which are predicted to be natively disordered. In addition, we determined the cell-cycle dependence of the phosphorylation of these sites by using stable isotope labeling and MS(2) analysis. Measurement of the site-specific phosphorylation ratios between mitotic and G(1) cells led us to conclude that several phosphorylation events of the subcomplex are mainly mitotic. Based on these results and our finding that the entire Nup107-160 subcomplex is stable throughout the cell cycle, we propose that phosphorylation does not affect interactions within the Nup107-160 subcomplex, but regulates the association of the subcomplex with the NPC and other proteins.
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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.