ArticleNature structural & molecular biology2021
The tertiary structure of the human Xkr8-Basigin complex that scrambles phospholipids at plasma membranes.
Article in Nature structural & molecular biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 45 citations in OpenAlex.
- The SLC-ome of membrane transport: from molecular discovery to physiology and clinical applications.Physiological reviews · 2026Review
- Article
- Lipid asymmetry disruption by XKR8 orchestrates neutrophil extracellular trap formation and inhibits fungal infection.Nature immunology · 2026Article
- Article
- CD147/Basigin: From Integrative Molecular Hub to Translational Therapeutic Target.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Review
- CD45 and Basigin (CD147) Are Functional Ligands for Galectin-8 on Human Leukocytes.Biomolecules · 2025Article
- Structure and function of the human apoptotic scramblase Xkr4.Nature communications · 2025Article
- A large-scale curated and filterable dataset for cryo-EM foundation model pre-training.Scientific data · 2025Article
- A basigin antibody modulates MCTs to impact tumor metabolism and immunity.Cell discovery · 2025Article
- Dys-regulated phosphatidylserine externalization as a cell intrinsic immune escape mechanism in cancer.Cell communication and signaling : CCS · 2025Review
- Membrane structure-responsive lipid scrambling by TMEM63B to control plasma membrane lipid distribution.Nature structural & molecular biology · 2025Article
- TMEM16 and OSCA/TMEM63 proteins share a conserved potential to permeate ions and phospholipids.eLife · 2024Article
- TMEM16 and OSCA/TMEM63 proteins share a conserved potential to permeate ions and phospholipids.bioRxiv : the preprint server for biology · 2024Article
- In or out of the groove? Mechanisms of lipid scrambling by TMEM16 proteins.Cell calcium · 2024Review
- Extracellular calcium functions as a molecular glue for transmembrane helices to activate the scramblase Xkr4.Nature communications · 2023Article
- Lipid scrambling is a general feature of protein insertases.bioRxiv : the preprint server for biology · 2023Article
- Lipid scrambling in immunology: why it is important.Cellular & molecular immunology · 2023Article
- Regulation of phospholipid distribution in the lipid bilayer by flippases and scramblases.Nature reviews. Molecular cell biology · 2023Review
- Phospholipid scramblase Xkr8 is required for developmental axon pruning via phosphatidylserine exposure.The EMBO journal · 2023Article
- Article
Corrections and comments
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Authors and funding
13 authors at 5 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Xkr8-Basigin is a plasma membrane phospholipid scramblase activated by kinases or caspases. We combined cryo-EM and X-ray crystallography to investigate its structure at an overall resolution of 3.8 Å. Its membrane-spanning region carrying 22 charged amino acids adopts a cuboid-like structure stabilized by salt bridges between hydrophilic residues in transmembrane helices. Phosphatidylcholine binding was observed in a hydrophobic cleft on the surface exposed to the outer leaflet of the plasma membrane. Six charged residues placed from top to bottom inside the molecule were essential for scrambling phospholipids in inward and outward directions, apparently providing a pathway for their translocation. A tryptophan residue was present between the head group of phosphatidylcholine and the extracellular end of the path. Its mutation to alanine made the Xkr8-Basigin complex constitutively active, indicating that it plays a vital role in regulating its scramblase activity. The structure of Xkr8-Basigin provides insights into the molecular mechanisms underlying phospholipid scrambling.
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Registered trials
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.