ArticleProceedings of the National Academy of Sciences of the United States of America2018
Structural basis of sterol recognition and nonvesicular transport by lipid transfer proteins anchored at membrane contact sites.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers, 1 of them a synthesis that pooled it.
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Who cites it
45 citing papers in PubMed, 1 synthesis or guideline pooled it, 85 citations in OpenAlex.
- Stay in touch with the endoplasmic reticulum.Science China. Life sciences · 2024Pooled it
- Sterol binding mechanism of a plant START-like domain: A new sterol transport paradigm via an amphiphilic cavity.The FEBS journal · 2026Article
- A dynamic feedback loop between retrograde sterol transport and TORC2 controls adaptation of the plasma membrane to stress.The EMBO journal · 2025Article
- Inhibition of OSBP blocks retrograde trafficking by inducing partial Golgi degradation.Nature chemical biology · 2025Article
- Mechanisms underlying targeted mitochondrial therapy for programmed cardiac cell death.Frontiers in physiology · 2025Review
- Insights into the role of sterol metabolism in antifungal drug resistance: a mini-review.Frontiers in microbiology · 2024Review
- Lysosomal membrane contact sites: Integrative hubs for cellular communication and homeostasis.Current topics in membranes · 2024Review
- Visualization of accessible cholesterol using a GRAM domain-based biosensor.Nature communications · 2023Article
- Regulation of cellular cholesterol distribution via non-vesicular lipid transport at ER-Golgi contact sites.Nature communications · 2023Article
- The History and Science of the Major Birch Pollen Allergen Bet v 1.Biomolecules · 2023Review
- Domain swapping of the C-terminal helix promotes the dimerization of a novel ribonuclease protein from Mycobacterium tuberculosis.Protein science : a publication of the Protein Society · 2023Article
- Optimization of Campesterol-Producing Yeast Strains as a Feasible Platform for the Functional Reconstitution of Plant Membrane-Bound Enzymes.ACS synthetic biology · 2023Article
- Cholesterol Transport to the Endoplasmic Reticulum.Cold Spring Harbor perspectives in biology · 2023Review
- Allosterically coupled conformational dynamics in solution prepare the sterol transfer protein StarD4 to release its cargo upon interaction with target membranes.Frontiers in molecular biosciences · 2023Article
- The role of extended synaptotagmin at membrane contact sites in cancer research.Frontiers in cell and developmental biology · 2023Review
- Transmembrane Membrane Readers form a Novel Class of Proteins That Include Peripheral Phosphoinositide Recognition Domains and Viral Spikes.Membranes · 2022Review
- Hepatocyte-Derived Prostaglandin E2-Modulated Macrophage M1-Type Polarization via mTOR-NPC1 Axis-Regulated Cholesterol Transport from Lysosomes to the Endoplasmic Reticulum in Hepatitis B Virus x Protein-Related Nonalcoholic Steatohepatitis.International journal of molecular sciences · 2022Article
- DeepContact: High-throughput quantification of membrane contact sites based on electron microscopy imaging.The Journal of cell biology · 2022Article
- Sterolight as imaging tool to study sterol uptake, trafficking and efflux in living cells.Scientific reports · 2022Article
- A VASt-domain protein regulates autophagy, membrane tension, and sterol homeostasis in rice blast fungus.Autophagy · 2021Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Membrane contact sites (MCSs) in eukaryotic cells are hotspots for lipid exchange, which is essential for many biological functions, including regulation of membrane properties and protein trafficking. Lipid transfer proteins anchored at membrane contact sites (LAMs) contain sterol-specific lipid transfer domains [StARkin domain (SD)] and multiple targeting modules to specific membrane organelles. Elucidating the structural mechanisms of targeting and ligand recognition by LAMs is important for understanding the interorganelle communication and exchange at MCSs. Here, we determined the crystal structures of the yeast Lam6 pleckstrin homology (PH)-like domain and the SDs of Lam2 and Lam4 in the apo form and in complex with ergosterol. The Lam6 PH-like domain displays a unique PH domain fold with a conserved N-terminal α-helix. The Lam6 PH-like domain lacks the basic surface for phosphoinositide binding, but contains hydrophobic patches on its surface, which are critical for targeting to endoplasmic reticulum (ER)-mitochondrial contacts. Structures of the LAM SDs display a helix-grip fold with a hydrophobic cavity and a flexible Ω1-loop as a lid. Ergosterol is bound to the pocket in a head-down orientation, with its hydrophobic acyl group located in the tunnel entrance. The Ω1-loop in an open conformation is essential for ergosterol binding by direct hydrophobic interaction. Structural comparison suggested that the sterol binding mode of the Lam2 SD2 is likely conserved among the sterol transfer proteins of the StARkin superfamily. Structural models of full-length Lam2 correlated with the sterol transport function at the membrane contact sites.
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