ArticleThe Journal of biological chemistry2015
Systemic RNA Interference Deficiency-1 (SID-1) Extracellular Domain Selectively Binds Long Double-stranded RNA and Is Required for RNA Transport by SID-1.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 64 citations in OpenAlex.
- Self-Assembling Nanoparticle Enhances RNA Interference Efficiency againstJournal of agricultural and food chemistry · 2026Article
- Harnessing microbial tools: Escherichia coli as a vehicle for neuropeptide functional analysis in Caenorhabditis elegans.Genetics · 2026Article
- Insect immune systems: same same but different but still same.Frontiers in immunology · 2026Review
- Bacterial RNA promotes proteostasis through inter-tissue communication in C. elegans.Nature communications · 2025Article
- Recent advances in understanding of the mechanisms of RNA interference in insects.Insect molecular biology · 2025Review
- Article
- Multispanning membrane protein SIDT2 increases knockdown activity of gapmer antisense oligonucleotides.Scientific reports · 2025Article
- Structure of the human systemic RNAi defective transmembrane protein 1 (hSIDT1) reveals the conformational flexibility of its lipid binding domain.Life science alliance · 2024Article
- Structural basis for double-stranded RNA recognition by SID1.Nucleic acids research · 2024Article
- Structure of the human systemic RNAi defective transmembrane protein 1 (hSIDT1) reveals the conformational flexibility of its lipid binding domain.bioRxiv : the preprint server for biology · 2024Article
- Cryo-EM analysis reveals human SID-1 transmembrane family member 1 dynamics underlying lipid hydrolytic activity.Communications biology · 2024Article
- Cryo-EM structures of human SID-1 transmembrane family proteins and implications for their low-pH-dependent RNA transport activity.Cell research · 2024Article
- Inheritance of Stress Responses via Small Non-Coding RNAs in Invertebrates and Mammals.Epigenomes · 2023Review
- A Tale of Two Lobsters-Transcriptomic Analysis Reveals a Potential Gap in the RNA Interference Pathway in the Tropical Rock LobsterInternational journal of molecular sciences · 2022Article
- Discovery and Use of Long dsRNA Mediated RNA Interference to Stimulate Antiviral Protection in Interferon Competent Mammalian Cells.Frontiers in immunology · 2022Article
- A Transcriptomic Study Reveals That Fish Vibriosis Due to the Zoonotic PathogenFrontiers in microbiology · 2022Article
- Establishing RNAi for basic research and pest control and identification of the most efficient target genes for pest control: a brief guide.Frontiers in zoology · 2021Review
- Genome-Wide Association Study Identifies a FunctionalArteriosclerosis, thrombosis, and vascular biology · 2021Article
- Article
- Examining the evidence for extracellular RNA function in mammals.Nature reviews. Genetics · 2021Review
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
During systemic RNA interference (RNAi) in Caenorhabditis elegans, RNA spreads across different cells and tissues in a process that requires the systemic RNA interference deficient-1 (sid-1) gene, which encodes an integral membrane protein. SID-1 acts cell-autonomously and is required for cellular import of interfering RNAs. Heterologous expression of SID-1 in Drosophila Schneider 2 cells enables passive uptake of dsRNA and subsequent soaking RNAi. Previous studies have suggested that SID-1 may serve as an RNA channel, but its precise molecular role remains unclear. To test the hypothesis that SID-1 mediates a direct biochemical recognition of RNA molecule and subsequent permeation, we expressed the extracellular domain (ECD) of SID-1 and purified it to near homogeneity. Recombinant purified SID-1 ECD selectively binds dsRNA but not dsDNA in a length-dependent and sequence-independent manner. Genetic missense mutations in SID-1 ECD causal for deficient systemic RNAi resulted in significant reduction in its affinity for dsRNA. Furthermore, full-length proteins with these mutations decrease SID-1-mediated RNA transport efficiency, providing evidence that dsRNA binding to SID-1 ECD is related to RNA transport. To examine the functional similarity of mammalian homologs of SID-1 (SIDT1 and SIDT2), we expressed and purified mouse SIDT1 and SIDT2 ECDs. We show that they bind long dsRNA in vitro, supportive of dsRNA recognition. In summary, our study illustrates the functional importance of SID-1 ECD as a dsRNA binding domain that contributes to RNA transport.
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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.