LC3/GABARAP binding to fluid membranes is potentiated by ceramide.
Yaiza R VarelaAlicia AlonsoPublished in: Autophagy (2022)
LC3/GABARAP constitute a macroautophagy/autophagy-related protein family derived from yeast Atg8. The involvement of specific lipids in LC3/GABARAP function is poorly understood. Exploring the interaction of LC3/GABARAP proteins with phosphatidylcholine- or sphingomyelin-based bilayers has revealed that cardiolipin is essential for the protein-bilayer interaction, and that ceramide markedly increases binding. Giant unilamellar vesicles examined under confocal fluorescence microscopy reveal that ceramide segregates laterally into very rigid domains, while GABARAP binds only the more fluid regions, suggesting that the enhancing role of ceramide is exerted by the minority of ceramide molecules dispersed in the fluid phase. Abbreviations: Atg8: autophagy-related 8; Cer: ceramide; CL: cardiolipin; eCer: egg ceramide; GABARAP: gamma-aminobutyric acid receptor associated protein; GUV: giant unilamellar vesicle; MAP1LC3/LC3: microtubule-associated protein 1 light chain 3; Rho-PE: lissamine rhodamine phosphatidylethanolamine; SM: sphingomyelin.
Keyphrases
- simultaneous determination
- mass spectrometry
- cell death
- liquid chromatography
- oxidative stress
- single molecule
- signaling pathway
- endoplasmic reticulum stress
- solid phase extraction
- high resolution
- gene expression
- optical coherence tomography
- single cell
- high throughput
- high speed
- transcription factor
- high density
- high resolution mass spectrometry
- saccharomyces cerevisiae
- amino acid