ArticleHuman molecular genetics2008
TDRD3, a novel Tudor domain-containing protein, localizes to cytoplasmic stress granules.
Article in Human molecular genetics, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 77 papers.
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Who cites it
77 citing papers in PubMed, 115 citations in OpenAlex.
- RECQ4 arginine methylation suppresses single-stranded DNA gap accumulation at replication forks.Nucleic acids research · 2026Article
- A genetic interaction between DED1 and HAT1 in Saccharomyces cerevisiae reveals a role for Hat1p in cytoplasmic RNA granule accumulation.G3 (Bethesda, Md.) · 2026Article
- TDRD3, a Tudor domain-containing protein, regulatesScience advances · 2026Article
- Article
- Deciphering the genetic basis of chlorophyll fluorescence parameters and vegetation indices under heat stress in blueberry.BMC plant biology · 2025Article
- Arginine methylation-dependent METTL14-SMN interaction regulates RNA mEMBO reports · 2025Article
- TDRD3 functions as a selective autophagy receptor with dual roles in autophagy and modulation of stress granule stability.bioRxiv : the preprint server for biology · 2024Article
- R-Methylation in Plants: A Key Regulator of Plant Development and Response to the Environment.International journal of molecular sciences · 2024Review
- The TDRD3-USP9X complex and MIB1 regulate TOP3B homeostasis and prevent deleterious TOP3B cleavage complexes.Nature communications · 2023Article
- Protein arginine methylation in transcription and epigenetic regulation.Frontiers in epigenetics and epigenomics · 2023Review
- Phase separation in innate immune response and inflammation-related diseases.Frontiers in immunology · 2023Review
- SMA-linked SMN mutants prevent phase separation properties and SMN interactions with FMRP family members.Life science alliance · 2023Article
- Stress Granules Determine the Development of Obesity-Associated Pancreatic Cancer.Cancer discovery · 2022Article
- TDRD3 is an antiviral restriction factor that promotes IFN signaling with G3BP1.PLoS pathogens · 2022Article
- Advances in the phase separation-organized membraneless organelles in cells: a narrative review.Translational cancer research · 2021Review
- Response to stress in biological disorders: Implications of stress granule assembly and function.Cell proliferation · 2021Review
- Article
- Arginine methylation of SARS-Cov-2 nucleocapsid protein regulates RNA binding, its ability to suppress stress granule formation, and viral replication.The Journal of biological chemistry · 2021Article
- Molecular Evolution of DNA Topoisomerase III Beta (TOP3B) in Metazoa.Journal of molecular evolution · 2021Article
- Stress Granules Involved in Formation, Progression and Metastasis of Cancer: A Scoping Review.Frontiers in cell and developmental biology · 2021Article
17 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Our previous work has demonstrated that the Tudor domain of the 'survival of motor neuron' protein and the Tudor domain-containing protein 3 (TDRD3) are highly similar and that they both have the ability to interact with arginine-methylated polypeptides. TDRD3 has been identified among genes whose overexpression has a strong predictive value for poor prognosis of estrogen receptor-negative breast cancers, although its precise function remains unknown. TDRD3 is a modular protein, and in addition to its Tudor domain, it harbors a putative nucleic acid recognition motif and a ubiquitin-associated domain. We report here that TDRD3 localizes predominantly to the cytoplasm, where it co-sediments with the fragile X mental retardation protein on actively translating polyribosomes. We also demonstrate that TDRD3 accumulates into stress granules (SGs) in response to various cellular stresses. Strikingly, the Tudor domain of TDRD3 was found to be both required and sufficient for its recruitment to SGs, and the methyl-binding surface in the Tudor domain is important for this process. Pull down experiments identified five novel TDRD3 interacting partners, most of which are potentially methylated RNA-binding proteins. Our findings revealed that two of these proteins, SERPINE1 mRNA-binding protein 1 and DEAD/H box-3 (a gene often deleted in Sertoli-cell-only syndrome), are also novel constituents of cytoplasmic SGs. Taken together, we report the first characterization of TDRD3 and its functional interaction with at least two proteins implicated in human genetic diseases and present evidence supporting a role for arginine methylation in the regulation of SG dynamics.
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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.