ArticlePLoS genetics2022
The Caenorhabditis elegans TDRD5/7-like protein, LOTR-1, interacts with the helicase ZNFX-1 to balance epigenetic signals in the germline.
Article in PLoS genetics, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
17 citing papers in PubMed, 25 citations in OpenAlex.
- Systematic identification of germ granule proteins reveals specialized roles in RNAi and small RNA inheritance.Genes & development · 2026Article
- Systematic Identification of Germ Granule Proteins Reveals Specialized Roles in RNAi and Small RNA Inheritance.bioRxiv : the preprint server for biology · 2026Article
- A SET domain-containing protein and HCF-1 maintain transgenerational epigenetic memory.Nature communications · 2026Article
- TurboID-based proximity labeling identifies novel germline proteins that maintain E granule integrity and small RNA homeostasis in C. elegans.Science China. Life sciences · 2025Article
- RG motifs promote piRNA-mediated gene silencing in C. elegans.Nucleic acids research · 2025Article
- Remodeling of Germ Cell mRNPs for Translational Control.Biology · 2025Review
- A nuclear pore-anchored condensate enables germ granule organization and transgenerational epigenetic inheritance.Nature structural & molecular biology · 2025Article
- piRNA processing within non-membrane structures is governed by constituent proteins and their functional motifs.The FEBS journal · 2025Review
- Two eIF4E paralogs occupy separate germ granule messenger ribonucleoproteins that mediate mRNA repression and translational activation.Genetics · 2025Article
- Repression of ZNFX1 by LncRNA ZFAS1 mediates tobacco-induced pulmonary carcinogenesis.Cellular & molecular biology letters · 2025Article
- ZNFX1: a multifunctional modulator of the innate immune response.Frontiers in immunology · 2025Review
- HERD-1 mediates multiphase condensate immiscibility to regulate small RNA-driven transgenerational epigenetic inheritance.Nature cell biology · 2024Article
- Caenorhabditis elegans germ granules are present in distinct configurations and assemble in a hierarchical manner.Development (Cambridge, England) · 2023Article
- sRNAfrag: a pipeline and suite of tools to analyze fragmentation in small RNA sequencing data.Briefings in bioinformatics · 2023Article
- C. elegans germ granules sculpt both germline and somatic RNAome.Nature communications · 2023Article
- Review
- Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
18 authors at 4 institutions in 3 countries.
Funding
Abstract
LOTUS and Tudor domain containing proteins have critical roles in the germline. Proteins that contain these domains, such as Tejas/Tapas in Drosophila, help localize the Vasa helicase to the germ granules and facilitate piRNA-mediated transposon silencing. The homologous proteins in mammals, TDRD5 and TDRD7, are required during spermiogenesis. Until now, proteins containing both LOTUS and Tudor domains in Caenorhabditis elegans have remained elusive. Here we describe LOTR-1 (D1081.7), which derives its name from its LOTUS and Tudor domains. Interestingly, LOTR-1 docks next to P granules to colocalize with the broadly conserved Z-granule helicase, ZNFX-1. The Tudor domain of LOTR-1 is required for its Z-granule retention. Like znfx-1 mutants, lotr-1 mutants lose small RNAs from the 3' ends of WAGO and mutator targets, reminiscent of the loss of piRNAs from the 3' ends of piRNA precursor transcripts in mouse Tdrd5 mutants. Our work shows that LOTR-1 acts with ZNFX-1 to bring small RNA amplifying mechanisms towards the 3' ends of its RNA templates.
Indexed as
Identifiers
What OpenQuestion holds
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.