ArticleNature communications2023
Structural insight into the human SID1 transmembrane family member 2 reveals its lipid hydrolytic activity.
Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 33 citations in OpenAlex.
- Article
- Glycosylated RNAs: discovery and implications in cancer biology.Frontiers in oncology · 2026Review
- The lysosomal catabolism of nucleic acids-critical regulators of the innate immune system.Nucleic acids research · 2025Review
- DHX8 regulates degradation of RNA by RNautophagy.Nucleic acids research · 2025Article
- Article
- Unraveling the Complex Genomic Interplay of Sickle Cell Disease Among the Saudi Population: A Case-Control GWAS Analysis.International journal of molecular sciences · 2025Article
- Multispanning membrane protein SIDT2 increases knockdown activity of gapmer antisense oligonucleotides.Scientific reports · 2025Article
- Role of glycoproteins in hepatic lipid metabolism: emerging diagnostic markers and therapeutic targets.PeerJ · 2025Review
- Genomics-driven drug repurposing and novel targets identification for sickle cell disease in Saudi patients.Frontiers in bioinformatics · 2025Article
- Regulatory mechanisms of acetic acid, ethanol and high temperature tolerances of acetic acid bacteria during vinegar production.Microbial cell factories · 2024Review
- 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 insights into double-stranded RNA recognition and transport by SID-1.Nature structural & molecular biology · 2024Article
- Cryo-EM structure reveals how SID-1 recognizes dsRNA that initiates systemic RNAi.Nature structural & molecular biology · 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
- Structural insights into cholesterol transport and hydrolase activity of a putative human RNA transport protein SIDT1.Cell discovery · 2024Article
- Human SIDT1 mediates dsRNA uptake via its phospholipase activity.Cell research · 2024Article
- Leveraging the transcriptome to further our understanding of GWAS findings: eQTLs associated with genes related to LDL and LDL subclasses, in a cohort of African Americans.Frontiers in genetics · 2024Article
- Cryo-EM structures of human SID-1 transmembrane family proteins and implications for their low-pH-dependent RNA transport activity.Cell research · 2024Article
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The systemic RNAi-defective (SID) transmembrane family member 2 (SIDT2) is a putative nucleic acid channel or transporter that plays essential roles in nucleic acid transport and lipid metabolism. Here, we report the cryo-electron microscopy (EM) structures of human SIDT2, which forms a tightly packed dimer with extensive interactions mediated by two previously uncharacterized extracellular/luminal β-strand-rich domains and the unique transmembrane domain (TMD). The TMD of each SIDT2 protomer contains eleven transmembrane helices (TMs), and no discernible nucleic acid conduction pathway has been identified within the TMD, suggesting that it may act as a transporter. Intriguingly, TM3-6 and TM9-11 form a large cavity with a putative catalytic zinc atom coordinated by three conserved histidine residues and one aspartate residue lying approximately 6 Å from the extracellular/luminal surface of the membrane. Notably, SIDT2 can hydrolyze C18 ceramide into sphingosine and fatty acid with a slow rate. The information presented advances the understanding of the structure-function relationships in the SID1 family proteins.
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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 Socratic graph.