ArticleNucleus (Austin, Tex.)2012
Two distinct sites in Nup153 mediate interaction with the SUMO proteases SENP1 and SENP2.
Article in Nucleus (Austin, Tex.), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 44 citations in OpenAlex.
- SUMOylation enhances DNMT1 function to repress mega-intergenic RNAs and viral mimicry.Nature genetics · 2026Article
- Synaptonemal complex SUMOylation is maintained by Nup60-dependent docking of Ulp1 at the nuclear periphery.Cell reports · 2026Article
- The role of phase separation for RNA and protein transport through the nuclear pore complex.Journal of experimental botany · 2026Review
- DNA double strand break repair: a model of specificity and complexity in SUMO signalling.Essays in biochemistry · 2025Review
- Ulp1 association with nuclear pore complexes is required for the maintenance of global SUMOylation.Molecular biology of the cell · 2025Article
- SUMOylation balance: a key determinant in synapse physiology.Frontiers in physiology · 2025Review
- Advances in the understanding of nuclear pore complexes in human diseases.Journal of cancer research and clinical oncology · 2024Review
- A role for Nup153 in nuclear assembly reveals differential requirements for targeting of nuclear envelope constituents.Molecular biology of the cell · 2022Article
- Structure, Maintenance, and Regulation of Nuclear Pore Complexes: The Gatekeepers of the Eukaryotic Genome.Cold Spring Harbor perspectives in 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
- Review
- Nucleoporin 153 links nuclear pore complex to chromatin architecture by mediating CTCF and cohesin binding.Nature communications · 2020Article
- K6-linked SUMOylation of BAF regulates nuclear integrity and DNA replication in mammalian cells.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- SUMO Protease SMT7 Modulates Ribosomal Protein L30 and Regulates Cell-Size Checkpoint Function.The Plant cell · 2020Article
- SUMOylation of the nuclear pore complex basket is involved in sensing cellular stresses.Journal of cell science · 2019Article
- SUMO-Mediated Regulation of Nuclear Functions and Signaling Processes.Molecular cell · 2018Review
- The SUMO-specific isopeptidase SENP2 is targeted to intracellular membranes via a predicted N-terminal amphipathic α-helix.Molecular biology of the cell · 2018Article
- Temporal and SUMO-specific SUMOylation contribute to the dynamics of Polo-like kinase 1 (PLK1) and spindle integrity during mouse oocyte meiosis.Developmental biology · 2018Article
- HOXA repression is mediated by nucleoporin Nup93 assisted by its interactors Nup188 and Nup205.Epigenetics & chromatin · 2016Article
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Authors and funding
4 authors at 2 institutions in 3 countries.
Funding
Abstract
Numerous enzymes of the mammalian SUMO modification pathway, including two members of the SUMO protease family, SENP2 and SENP1, localize to the nuclear periphery. The SUMO proteases play roles both in processing SUMO during the biogenesis of this peptide moiety and also in reversing SUMO modification on specific targets to control the activities conferred by this post-translational modification. Although interaction with the C-terminal domain of the nucleoporin Nup153 is thought to contribute to SENP2 localization at the nuclear pore complex, little is known about the binding partners of SENP1 at the nuclear periphery. We have found that Nup153 binds to both SENP1 and SENP2 and does so by interacting with the unique N-terminal domain of Nup153 as well as a specific region within the C-terminal FG-rich region. We have further found that Nup153 is a substrate for sumoylation, with this modification kept in check by these two SUMO proteases. Specifically, either RNAi depletion of SENP1/SENP2 or expression of dominantly interfering mutants of these proteins results in increased sumoylation of endogenous Nup153. While SENP1 and SENP2 share many characteristics, we show here that SENP1 levels are influenced by the presence of Nup153, whereas SENP2 is not sensitive to changes in Nup153 abundance.
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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.