ArticleThe Journal of biological chemistry2019
The 40S ribosomal protein uS5 (RPS2) assembles into an extraribosomal complex with human ZNF277 that competes with the PRMT3-uS5 interaction.
Article in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 31 citations in OpenAlex.
- The N-terminal extension of ribosomal protein Rps2 shapes its early fate through Chaperone-Importin competition and arginine methylation.The Journal of biological chemistry · 2026Article
- Draft Genome Assembly and Differential Expression ofPlants (Basel, Switzerland) · 2026Article
- Estrogen-Induced Hypermethylation Silencing ofCells · 2026Article
- PRMT3 in cancer: arginine methylation as a driver of tumor metabolism, immune evasion, and therapeutic resistance.Frontiers in immunology · 2026Review
- Emerging roles of protein arginine methyltransferase in multiple myeloma.Molecular therapy. Oncology · 2025Review
- Drosophila Trus, the orthologue of mammalian PDCD2L, is required for proper cell proliferation, larval developmental timing, and oogenesis.PLoS genetics · 2025Article
- PRMT3 and CARM1: Emerging Epigenetic Targets in Cancer.Journal of cellular and molecular medicine · 2025Review
- Expression Profiles of Housekeeping Genes and Tissue-Specific Genes in Different Tissues of Chinese Sturgeon (Animals : an open access journal from MDPI · 2024Article
- Reconsideration of the laminin receptor 67LR in colorectal cancer cells.Biomolecules & biomedicine · 2024Article
- Programmed Cell Death Protein 2-like Promotes Inflammation and Oxidative Stress in Vascular Endothelial Cells.ACS pharmacology & translational science · 2023Article
- Tudor-dimethylarginine interactions: the condensed version.Trends in biochemical sciences · 2023Review
- Dissecting the Nuclear Import of the Ribosomal Protein Rps2 (uS5).Biomolecules · 2023Article
- Ribosomal Protein uS5 and Friends: Protein-Protein Interactions Involved in Ribosome Assembly and Beyond.Biomolecules · 2023Review
- PABPN1 prevents the nuclear export of an unspliced RNA with a constitutive transport element and controls human gene expression via intron retention.RNA (New York, N.Y.) · 2023Article
- A ZTF-7/RPS-2 complex mediates the cold-warm response in C. elegans.PLoS genetics · 2023Article
- PRMT3 drives glioblastoma progression by enhancing HIF1A and glycolytic metabolism.Cell death & disease · 2022Article
- A proteogenomic signature of age-related macular degeneration in blood.Nature communications · 2022Article
- Localization and Functional Roles of Components of the Translation Apparatus in the Eukaryotic Cell Nucleus.Cells · 2021Review
- Mechanisms of Cotranslational Protein Maturation in Bacteria.Frontiers in molecular biosciences · 2021Review
- PDCD2 functions as an evolutionarily conserved chaperone dedicated for the 40S ribosomal protein uS5 (RPS2).Nucleic acids research · 2020Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Ribosomal (r)-proteins are generally viewed as ubiquitous, constitutive proteins that simply function to maintain ribosome integrity. However, findings in the past decade have led to the idea that r-proteins have evolved specialized functions beyond the ribosome. For example, the 40S ribosomal protein uS5 (RPS2) is known to form an extraribosomal complex with the protein arginine methyltransferase PRMT3 that is conserved from fission yeast to humans. However, the full scope of uS5's extraribosomal functions, including whether uS5 interacts with any other proteins, is not known. In this study, we identify the conserved zinc finger protein 277 (ZNF277) as a new uS5-associated protein by using quantitative proteomics approaches in human cells. As previously shown for PRMT3, we found that ZNF277 uses a C2H2-type zinc finger domain to recognize uS5. Analysis of protein-protein interactions in living cells indicated that the ZNF277-uS5 complex is found in the cytoplasm and the nucleolus. Furthermore, we show that ZNF277 and PRMT3 compete for uS5 binding, because overexpression of PRMT3 inhibited the formation of the ZNF277-uS5 complex, whereas depletion of cellular ZNF277 resulted in increased levels of uS5-PRMT3. Notably, our results reveal that ZNF277 recognizes nascent uS5 in the course of mRNA translation, suggesting cotranslational assembly of the ZNF277-uS5 complex. Our findings thus unveil an intricate network of evolutionarily conserved protein-protein interactions involving extraribosomal uS5, suggesting a key role for uS5 beyond the ribosome.
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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.