ArticleFrontiers in cell and developmental biology2022
Structural Predictions of the SNX-RGS Proteins Suggest They Belong to a New Class of Lipid Transfer Proteins.
Article in Frontiers in cell and developmental biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 27 citations in OpenAlex.
- Structural Organization of the Nvj3-Mdm1 Complex Reveals a Conserved Lipid-Compatible Contact Site Module.bioRxiv : the preprint server for biology · 2026Article
- Nvj3 regulates Dga1-mediated triacylglycerol synthesis and lipid droplet formation at ER contact sites.bioRxiv : the preprint server for biology · 2026Article
- From CASP13 to the Nobel Prize: DeepMind's AlphaFold Journey in Revolutionizing Protein Structure Prediction and Beyond.Current protein & peptide science · 2026Review
- Sphingolipid and methionine metabolism in aging.Journal of cell science · 2025Review
- Making lipids very unhappy to discover how they bind to proteins.The Journal of cell biology · 2024Article
- Unbiased MD simulations identify lipid binding sites in lipid transfer proteins.The Journal of cell biology · 2024Article
- Modular Structure and Polymerization Status of GABAInternational journal of molecular sciences · 2024Article
- Lipid droplets and fatty acid-induced lipotoxicity: in a nutshell.FEBS letters · 2024Article
- Altered lipid homeostasis is associated with cerebellar neurodegeneration in SNX14 deficiency.JCI insight · 2024Article
- Lysosomal membrane contact sites: Integrative hubs for cellular communication and homeostasis.Current topics in membranes · 2024Review
- Interaction of the sorting nexin 25 homologue Snazarus with Rab11 balances endocytic and secretory transport and maintains the ultrafiltration diaphragm in nephrocytes.Molecular biology of the cell · 2023Article
- The (social) lives, deaths, and biophysical phases of lipid droplets.Current opinion in cell biology · 2023Review
- Endoplasmic Reticulum Membrane Contact Sites, Lipid Transport, and Neurodegeneration.Cold Spring Harbor perspectives in biology · 2023Review
- AlphaFold2 and its applications in the fields of biology and medicine.Signal transduction and targeted therapy · 2023Review
- Exploring AlphaFold2's Performance on Predicting Amino Acid Side-Chain Conformations and Its Utility in Crystal Structure Determination of B318L Protein.International journal of molecular sciences · 2023Article
- Systematic analysis of membrane contact sites ineLife · 2022Article
- Vacuole-Specific Lipid Release for Tracking Intracellular Lipid Metabolism and Transport inACS chemical biology · 2022Article
- Present Impact of AlphaFold2 Revolution on Structural Biology, and an Illustration With the Structure Prediction of the Bacteriophage J-1 Host Adhesion Device.Frontiers in molecular biosciences · 2022Article
- Structural Organization of the Nvj3-Mdm1 Complex Reveals a Conserved Lipid-Compatible Contact Site Module.Contact (Thousand Oaks (Ventura County, Calif.))Article
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6 authors at 2 institutions in 2 countries.
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Abstract
Recent advances in protein structure prediction using machine learning such as AlphaFold2 and RosettaFold presage a revolution in structural biology. Genome-wide predictions of protein structures are providing unprecedented insights into their architecture and intradomain interactions, and applications have already progressed towards assessing protein complex formation. Here we present detailed analyses of the sorting nexin proteins that contain regulator of G-protein signalling domains (SNX-RGS proteins), providing a key example of the ability of AlphaFold2 to reveal novel structures with previously unsuspected biological functions. These large proteins are conserved in most eukaryotes and are known to associate with lipid droplets (LDs) and sites of LD-membrane contacts, with key roles in regulating lipid metabolism. They possess five domains, including an N-terminal transmembrane domain that anchors them to the endoplasmic reticulum, an RGS domain, a lipid interacting phox homology (PX) domain and two additional domains named the PXA and PXC domains of unknown structure and function. Here we report the crystal structure of the RGS domain of sorting nexin 25 (SNX25) and show that the AlphaFold2 prediction closely matches the experimental structure. Analysing the full-length SNX-RGS proteins across multiple homologues and species we find that the distant PXA and PXC domains in fact fold into a single unique structure that notably features a large and conserved hydrophobic pocket. The nature of this pocket strongly suggests a role in lipid or fatty acid binding, and we propose that these molecules represent a new class of conserved lipid transfer proteins.
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