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Visualizing suborganellar lipid distribution using correlative light and electron microscopy.

H Mathilda Lennartz1, Suman Khan2, Weihua Leng3

  • 1Max Planck Institute of Molecular Cell Biology and Genetics, Dresden, Germany. hlennart@mpi-cbg.de.

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|March 21, 2026
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Summary
This summary is machine-generated.

Researchers developed Lipid-CLEM, a new microscopy technique to visualize lipid nanoscale organization in cell membranes. This method reveals how lipids like sphingomyelin are organized within early endosomes, similar to proteins.

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Area of Science:

  • Cell Biology
  • Microscopy
  • Biochemistry

Background:

  • Biological membranes are organized into nanoscale domains crucial for cellular functions.
  • Understanding lipid and protein localization at the nanoscale is essential for studying these domains.
  • Existing methods for visualizing lipid localization at the nanoscale are insufficient.

Purpose of the Study:

  • To introduce a novel correlative light and electron microscopy (CLEM) workflow for imaging lipids (Lipid-CLEM).
  • To enable the quantification of relative lipid densities within membrane nanodomains.
  • To investigate the nanoscale organization of lipids in early endosomes.

Main Methods:

  • Developed a correlative light and electron microscopy workflow (Lipid-CLEM).
  • Utilized near-native lipid probes and on-section labelling via click chemistry.
  • Enabled simultaneous visualization and quantification of lipid and protein localization.

Main Results:

  • Demonstrated the ability to quantify relative lipid densities in membrane nanodomains.
  • Observed differential partitioning of sphingomyelin in early endosome compartments (intraluminal vesicles, recycling tubules, boundary membrane).
  • Revealed nanoscale lipid organization comparable to previously observed protein organization.

Conclusions:

  • The Lipid-CLEM workflow significantly advances the study of lipid localization at the nanoscale.
  • Provides mechanistic insights into lipid functions in cell biology.
  • Facilitates simultaneous investigation of proteins and lipids in membrane nanodomain assembly and function.