ArticleNature chemical biology2026
Leaflet-specific phospholipid imaging using genetically encoded proximity sensors.
Article in Nature chemical biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Bioorthogonal chemistry for deciphering lipid biology in living systems.RSC chemical biology · 2026Review
- Two-step mechanism of Bruton's tyrosine kinase membrane recruitment and activation.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Self-Assembling Cationic Lipopeptides for the Construction of Functional Vesicular Gene-Delivery Systems.Small (Weinheim an der Bergstrasse, Germany) · 2026Article
- How to catch a lipid transporter.Nature chemical biology · 2026Article
- Selective Editing and Functionalization of the Mammalian Lipidome.bioRxiv : the preprint server for biology · 2026Article
- Chemical biology approaches for revealing interorganelle lipid transport pathways.Current opinion in cell biology · 2026Review
- Unmasking the FACES of membrane bilayers.Nature chemical biology · 2026Article
- Two-Step Mechanism of Bruton's Tyrosine Kinase Membrane Recruitment and Activation.bioRxiv : the preprint server for biology · 2025Article
- Emerging Approaches for Studying Lipid Dynamics, Metabolism, and Interactions in Cells.Annual review of biochemistry · 2025Review
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11 authors.
Funding
Abstract
The lipid composition of cells varies widely across organelles and between individual membrane leaflets. Transport proteins are thought to generate this heterogeneity, but measuring their functions in vivo has been hampered by limited tools for imaging lipids at relevant spatial resolutions. Here we present fluorogen-activating coincidence encounter sensing (FACES), a chemogenetic tool capable of quantitatively imaging subcellular lipid pools and reporting their transbilayer orientation in living cells. FACES combines bioorthogonal chemistry with genetically encoded fluorogen-activating proteins (FAPs) for reversible proximity sensing of conjugated molecules. We first apply this approach to identify roles for lipid transfer proteins that traffic phosphatidylcholine pools between the ER and mitochondria. We then show that transmembrane domain-containing FAPs can reveal the membrane asymmetry of multiple lipid classes in the trans-Golgi network and be used to investigate the mechanisms that generate it. Finally, we present that FACES can be applied to measure glycans and other molecule classes.
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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.