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Triglycerides serve as crucial long-term energy storage molecules in microorganisms, providing a dense source of metabolic energy. Their breakdown is mediated by lipases, which hydrolyze triglycerides into glycerol and free fatty acids. Each of these components follows distinct metabolic pathways, ultimately contributing to ATP synthesis and cellular energy homeostasis.Glycerol MetabolismGlycerol, released from triglyceride hydrolysis, is phosphorylated by glycerol kinase to form...
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Lipid Vesicle-mediated Affinity Chromatography using Magnetic Activated Cell Sorting LIMACS: a Novel Method to Analyze Protein-lipid Interaction
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Chemical Probe-Enabled Lipid Droplet Proteomics.

Jing Xiang1, Tao Li1, Junzhe Zhang2

  • 1Department of Pharmacology, School of Basic Medical Sciences, Cheeloo College of Medicine, Shandong University, Jinan 250012, China.

Journal of the American Chemical Society
|March 11, 2025
PubMed
Summary

New chemical probes, LDF and LDPL, enable live-cell imaging and proteomic profiling of lipid droplets (LDs). LDPL allows large-scale LD proteome analysis without cell isolation, identifying key proteins involved in LD function and disease.

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Area of Science:

  • Cell Biology
  • Biochemistry
  • Chemical Biology

Background:

  • Lipid droplets (LDs) are crucial for lipid metabolism, energy balance, and cellular stress responses.
  • Dysregulation of LDs is implicated in diseases like obesity, cancer, and atherosclerosis.
  • Understanding the LD proteome is vital, but global profiling in live cells without isolation remains challenging.

Purpose of the Study:

  • To develop novel chemical probes for live-cell imaging and proteomic analysis of lipid droplets (LDs).
  • To establish a method for large-scale LD proteome profiling directly within native cellular environments.

Main Methods:

  • Development and application of two small-molecule chemical probes, LDF and LDPL.
  • Live-cell fluorescence imaging of LDs using LDF/LDPL in cells and animal tissues.
  • Large-scale proteomic profiling of LDs using LDPL without prior LD isolation.

Main Results:

  • LDF and LDPL enabled specific live-cell and tissue imaging of LDs.
  • LDPL facilitated the identification of 1584 high-confidence proteins associated with LD functions.
  • Validation studies identified CHMP6 as a lipophagy receptor and PRDX4 as a lipolysis suppressor.

Conclusions:

  • LDPL is a powerful chemical tool for in situ LD proteome profiling.
  • This novel strategy enhances understanding of LD proteomics in native cellular contexts.
  • The approach holds potential for deciphering LD dynamics and mechanisms in various diseases.