ArticleMolecular and cellular biology2004
SUMO modification of heterogeneous nuclear ribonucleoproteins.
Article in Molecular and cellular biology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.
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Who cites it
57 citing papers in PubMed, 111 citations in OpenAlex.
- Repurposed hnRNPC binds mature mRNAs and safeguards the mitotic transcriptome.Nucleic acids research · 2026Article
- The role of SUMOylation in biomolecular condensate dynamics and protein localization.Cell insight · 2024Review
- Rhes, a striatal enriched protein, regulates post-translational small-ubiquitin-like-modifier (SUMO) modification of nuclear proteins and alters gene expression.Cellular and molecular life sciences : CMLS · 2024Article
- Nucleo-cytoplasmic shuttling of 14-3-3 epsilon carrying hnRNP C promotes autophagy.Cancer biology & therapy · 2023Article
- Regulation of Pre-mRNA Splicing: Indispensable Role of Post-Translational Modifications of Splicing Factors.Life (Basel, Switzerland) · 2023Review
- SUMOylation of HNRNPA2B1 modulates RPA dynamics during unperturbed replication and genotoxic stress responses.Molecular cell · 2023Article
- CPEB3 low-complexity motif regulates local protein synthesis via protein-protein interactions in neuronal ribonucleoprotein granules.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- The scaffold protein IQGAP1 links heat-induced stress signals to alternative splicing regulation in gastric cancer cells.Oncogene · 2021Article
- Adenovirus-mediated ubiquitination alters protein-RNA binding and aids viral RNA processing.Nature microbiology · 2020Article
- Ubc9 Attenuates Myocardial Ischemic Injury Through Accelerating Autophagic Flux.Frontiers in pharmacology · 2020Article
- Alternative Splicing and DNA Damage Response in Plants.Frontiers in plant science · 2020Review
- Rotavirus Induces Formation of Remodeled Stress Granules and P Bodies and Their Sequestration in Viroplasms To Promote Progeny Virus Production.Journal of virology · 2018Article
- Cytoplasmic Relocalization and Colocalization with Viroplasms of Host Cell Proteins, and Their Role in Rotavirus Infection.Journal of virology · 2018Article
- A SUMO-dependent feedback loop senses and controls the biogenesis of nuclear pore subunits.Nature communications · 2018Article
- DNA damage-induced dynamic changes in abundance and cytosol-nuclear translocation of proteins involved in translational processes, metabolism, and autophagy.Cell cycle (Georgetown, Tex.) · 2018Article
- When SUMO met splicing.RNA biology · 2018Review
- SUMOylation Negatively Regulates Angiogenesis by Targeting Endothelial NOTCH Signaling.Circulation research · 2017Article
- Roles of Sumoylation in mRNA Processing and Metabolism.Advances in experimental medicine and biology · 2017Review
- A comprehensive compilation of SUMO proteomics.Nature reviews. Molecular cell biology · 2016Article
- Identification of cell-specific targets of sumoylation during mouse spermatogenesis.Reproduction (Cambridge, England) · 2016Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Small ubiquitin-related modifiers (SUMOs) are proteins that are posttranslationally conjugated to other cellular proteins, particularly those that localize and function in the nucleus. Enzymes regulating SUMO modification localize in part to nuclear pore complexes (NPCs), indicating that modification of some proteins may occur as they are translocated between the nucleus and the cytoplasm. Substrates that are regulated by SUMO modification at NPCs, however, have not been previously identified. Among the most abundant cargos transported through NPCs are the heterogeneous nuclear ribonucleoproteins (hnRNPs). HnRNPs are involved in various aspects of mRNA biogenesis, including regulation of pre-mRNA splicing and nuclear export. Here, we demonstrate that two subsets of hnRNPs, the hnRNP C and M proteins, are substrates for SUMO modification. We demonstrate that the hnRNP C proteins are modified by SUMO at a single lysine residue, K237, and that SUMO modification at this site decreases their binding to nucleic acids. We also show that Nup358, a SUMO E3 ligase associated with the cytoplasmic fibrils of NPCs, enhances the SUMO modification of the hnRNP C and M proteins. Based on our findings, we propose that SUMO modification of the hnRNP C and M proteins may occur at NPCs and facilitate the nucleocytoplasmic transport of mRNAs.
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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.