ArticleNucleic acids research2020
PDCD2 functions as an evolutionarily conserved chaperone dedicated for the 40S ribosomal protein uS5 (RPS2).
Article in Nucleic acids research, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 26 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
- Biosensor-guided discovery of peptide inhibitors targeting the ribosomal protein uS5-PDCD2 chaperone interaction.The Journal of biological chemistry · 2026Article
- PDCD2L overexpression represents an unfavorable prognostic marker and its inhibition shows promising therapeutic potential for gastric cancer.Cancer biomarkers : section A of Disease markers · 2025Article
- Drosophila Trus, the orthologue of mammalian PDCD2L, is required for proper cell proliferation, larval developmental timing, and oogenesis.PLoS genetics · 2025Article
- Biallelic variants in the conserved ribosomal protein chaperone geneProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Calcium Homeostasis Is Involved in the Modulation of Gene Expression by MSL2 in Imbalanced Genomes.Cells · 2024Article
- AtPRMT3-RPS2B promotes ribosome biogenesis and coordinates growth and cold adaptation trade-off.Nature communications · 2024Article
- PDCD2 as a prognostic biomarker in glioma correlates with malignant phenotype.Genes & diseases · 2024Article
- Article
- Proteomics-Based Discovery of First-in-Class Chemical Probes for Programmed Cell Death Protein 2 (PDCD2).Angewandte Chemie (International ed. in English) · 2023Article
- 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
- Heliangin acts as a covalent ligand of RPS2 that disrupts pre-rRNA metabolic processes inActa pharmaceutica Sinica. B · 2023Article
- Identification of PDCD2 as a Candidate Target of Andrographolide That Arrests the Tumor Cell Cycle by Human Proteome-Scale Screening.ACS pharmacology & translational science · 2022Article
- Release of the ribosome biogenesis factor Bud23 from small subunit precursors in yeast.RNA (New York, N.Y.) · 2022Article
- Cyclophilin acts as a ribosome biogenesis factor by chaperoning the ribosomal protein (PlRPS15) in filamentous fungi.Nucleic acids research · 2021Article
- The possible role of SRMS in colorectal cancer by bioinformatics analysis.World journal of surgical oncology · 2021Article
- Eukaryotic Ribosome Biogenesis: The 60S Subunit.Acta naturaeArticle
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
PDCD2 is an evolutionarily conserved protein with previously characterized homologs in Drosophila (zfrp8) and budding yeast (Tsr4). Although mammalian PDCD2 is essential for cell proliferation and embryonic development, the function of PDCD2 that underlies its fundamental cellular role has remained unclear. Here, we used quantitative proteomics approaches to define the protein-protein interaction network of human PDCD2. Our data revealed that PDCD2 specifically interacts with the 40S ribosomal protein uS5 (RPS2) and that the PDCD2-uS5 complex is assembled co-translationally. Loss of PDCD2 expression leads to defects in the synthesis of the small ribosomal subunit that phenocopy a uS5 deficiency. Notably, we show that PDCD2 is important for the accumulation of soluble uS5 protein as well as its incorporation into 40S ribosomal subunit. Our findings support that the essential molecular function of PDCD2 is to act as a dedicated ribosomal protein chaperone that recognizes uS5 co-translationally in the cytoplasm and accompanies uS5 to ribosome assembly sites in the nucleus. As most dedicated ribosomal protein chaperones have been identified in yeast, our study reveals that similar mechanisms exist in human cells to assist ribosomal proteins coordinate their folding, nuclear import and assembly in pre-ribosomal particles.
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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.