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Extraction of Extracellular Vesicles from Whole Tissue
Published on: February 7, 2019
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Lysophospholipids Facilitate COPII Vesicle Formation.
Alejandro Melero1, Nicolas Chiaruttini2, Takefumi Karashima3
1Department of Biochemistry, University of Geneva, 1211 Geneva, Switzerland; Swiss National Centre for Competence in Research in Chemical Biology, 1211 Geneva, Switzerland.
Current Biology : CB
|June 12, 2018
Summary
Phospholipase B3 overexpression partially restores cell growth and protein transport in a COPII mutant by increasing lysophosphatidylinositol (lysoPI). This lipid enhances COPII vesicle budding by reducing membrane rigidity.
Area of Science:
- Cell biology
- Membrane trafficking
- Lipid biochemistry
Background:
- Coat protein complex II (COPII) machinery mediates endoplasmic reticulum export.
- Sec12 acts as a guanine nucleotide exchange factor for Sar1 GTPase, initiating COPII assembly.
- Defects in COPII function impair protein transport and cell growth.
Purpose of the Study:
- Investigate the role of phospholipase B3 (PLB3) in a thermosensitive COPII mutant (sec12-4).
- Determine the impact of PLB3 on cell growth and protein transport under non-permissive conditions.
- Elucidate the mechanism by which PLB3 influences COPII vesicle formation.
Main Methods:
- Genetic manipulation (overexpression of PLB3 in sec12-4 mutant).
- Lipidomics analysis to quantify cellular lipid content.
- In vitro COPII vesicle budding assays.
- Liposome reconstitution assays with purified proteins.
Main Results:
- PLB3 overexpression partially restored growth and protein transport in the sec12-4 mutant.
- Lipidomics revealed increased lysophosphatidylinositol (lysoPI) levels in PLB3-overexpressing cells.
- lysoPI was enriched in isolated COPII vesicles and enhanced COPII recruitment to liposomes.
- lysoPI decreased membrane rigidity, facilitating COPII binding.
Conclusions:
- Lysophospholipids, specifically lysoPI, can mechanically facilitate COPII vesicle budding.
- PLB3-mediated lysoPI production offers a potential therapeutic strategy for COPII-related transport defects.
- This study reveals a novel role for lipids in regulating COPII coat dynamics.
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