ArticleProceedings of the National Academy of Sciences of the United States of America2020
Nonclassical nuclear localization signals mediate nuclear import of CIRBP.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.
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Who cites it
47 citing papers in PubMed, 69 citations in OpenAlex.
- Nucleosome Assembly Protein 1 in Dinoflagellate Cells Without Architectural Nucleosomes.International journal of molecular sciences · 2026Article
- Multiple roads between the nucleus and the cytoplasm: classes of linear NLSs and NESs and their receptors.Current opinion in structural biology · 2026Review
- Importin-9 recognizes the winged-helix fold of ETS transcription factors to mediate nuclear import.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Phase separation of PGL-3 driven by structured domains that oligomerize and interact with RGG motifs.EMBO reports · 2026Article
- Importins recognize the winged-helix fold of ETS transcription factors to mediate nuclear import.bioRxiv : the preprint server for biology · 2026Article
- Computational investigation of the sequence context of arginine/glycine-rich motifs in the human proteome.BMC genomics · 2025Article
- Nanocarrier-Based Systems for Targeted Delivery: Current Challenges and Future Directions.MedComm · 2025Review
- Structural basis of phosphorylation-independent nuclear import of CIRBP by TNPO3.Nature communications · 2025Article
- NLS-binding deficient Kapβ2 reduces neurotoxicity via selective interaction with C9orf72-ALS/FTD dipeptide repeats.Communications biology · 2025Article
- Nuclear trafficking ofVirus evolution · 2025Article
- Dysregulation of SRSF3/International journal of biological sciences · 2025Article
- Nuclear-Cytoplasmic Shuttling of the Usher Syndrome 1G Protein SANS Differs from Its Paralog ANKS4B.Cells · 2024Article
- The RNA-binding Selectivity of the RGG/RG Motifs of hnRNP U is Abolished by Elements Within the C-terminal Intrinsically Disordered Region.Journal of molecular biology · 2024Article
- Engineered NLS-chimera downregulates expression of aggregation-prone endogenous FUS.Nature communications · 2024Article
- Two ZnApplied and environmental microbiology · 2024Article
- An emerging role for the endoplasmic reticulum in stress granule biogenesis.Seminars in cell & developmental biology · 2024Review
- Nuclear-import receptors as gatekeepers of pathological phase transitions in ALS/FTD.Molecular neurodegeneration · 2024Review
- Chaperone regulation of biomolecular condensates.Frontiers in biophysics · 2024Article
- hnRNPs: roles in neurodevelopment and implication for brain disorders.Frontiers in molecular neuroscience · 2024Review
- Nuclear transport proteins: structure, function, and disease relevance.Signal transduction and targeted therapy · 2023Review
Corrections and comments
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Authors and funding
12 authors at 3 institutions in 2 countries.
Funding
Abstract
The specific interaction of importins with nuclear localization signals (NLSs) of cargo proteins not only mediates nuclear import but also, prevents their aberrant phase separation and stress granule recruitment in the cytoplasm. The importin Transportin-1 (TNPO1) plays a key role in the (patho-)physiology of both processes. Here, we report that both TNPO1 and Transportin-3 (TNPO3) recognize two nonclassical NLSs within the cold-inducible RNA-binding protein (CIRBP). Our biophysical investigations show that TNPO1 recognizes an arginine-glycine(-glycine) (RG/RGG)-rich region, whereas TNPO3 recognizes a region rich in arginine-serine-tyrosine (RSY) residues. These interactions regulate nuclear localization, phase separation, and stress granule recruitment of CIRBP in cells. The presence of both RG/RGG and RSY regions in numerous other RNA-binding proteins suggests that the interaction of TNPO1 and TNPO3 with these nonclassical NLSs may regulate the formation of membraneless organelles and subcellular localization of numerous proteins.
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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.