ArticleScientific reports2017
A novel family of mammalian transmembrane proteins involved in cholesterol transport.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 46 citations in OpenAlex.
- The SLC-ome of membrane transport: from molecular discovery to physiology and clinical applications.Physiological reviews · 2026Review
- Article
- Molecular pathogenesis of Alzheimer's disease onset in a mouse model: effects of cannabidiol treatment.Frontiers in neuroscience · 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 insights into double-stranded RNA recognition and transport by SID-1.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
- Analysis of cholesterol-recognition motifs of the plasma membrane CaJournal of bioenergetics and biomembranes · 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
- Gender Control of Mouse Embryos by Activation of TLR7/8 on X Sperm via Ligands dsRNA-40 and dsRNA-DR.Molecules (Basel, Switzerland) · 2024Article
- SIDT2 Associates with Apolipoprotein A1 (ApoA1) and Facilitates ApoA1 Secretion in Hepatocytes.Cells · 2023Article
- Structural insight into the human SID1 transmembrane family member 2 reveals its lipid hydrolytic activity.Nature communications · 2023Article
- Integrated regulation of dopaminergic and epigenetic effectors of neuroprotection in Parkinson's disease models.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Interaction betweenNutrients · 2023Article
- Persistent Parental RNAi in the BeetleAdvanced genetics (Hoboken, N.J.) · 2022Article
- Correlation of SIDT1 with Poor Prognosis and Immune Infiltration in Patients with Non-Small Cell Lung Cancer.International journal of general medicine · 2022Article
- Dissecting protein domain variability in the core RNA interference machinery of five insect orders.RNA biology · 2021Article
- Genome-Wide Association Study Identifies a FunctionalArteriosclerosis, thrombosis, and vascular biology · 2021Article
- Perturbing the Normal Level of SIDT1 Suppresses the Naked ASO Effect.Journal of nucleic acids · 2021Article
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Authors and funding
4 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cholesterol is an essential compound in mammalian cells because it is involved in a wide range of functions, including as a key component of membranes, precursor of important molecules such as hormones, bile acids and vitamin D. The cholesterol transport across the circulatory system is a well-known process in contrast to the intracellular cholesterol transport, which is poorly understood. Recently in our laboratory, we identified a novel protein in C. elegans involved in dietary cholesterol uptake, which we have named ChUP-1. Insillicoanalysis identified two putative orthologue candidate proteins in mammals. The proteins SIDT1 and SIDT2 share identity and conserved cholesterol binding (CRAC) domains with C. elegans ChUP-1. Both mammalian proteins are annotated as RNA transporters in databases. In the present study, we show evidence indicating that SIDT1 and SIDT2 not only do not transport RNA, but they are involved in cholesterol transport. Furthermore, we show that single point mutations directed to disrupt the CRAC domains of both proteins prevent FRET between SIDT1 and SIDT2 and the cholesterol analogue dehydroergosterol (DHE) and alter cholesterol 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.