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Lysophospholipids Facilitate COPII Vesicle Formation.

  • Melero A Department of Biochemistry, University of Geneva, 1211 Geneva, Switzerland; Swiss National Centre for Competence in Research in Chemical Biology, 1211 Geneva, Switzerland.
  • Chiaruttini N Department of Biochemistry, University of Geneva, 1211 Geneva, Switzerland.
  • Karashima T Department of Bioresource Science and Technology, Hiroshima University, Hiroshima 739-8528, Japan.
  • Riezman I Department of Biochemistry, University of Geneva, 1211 Geneva, Switzerland.
  • Funato K Department of Bioresource Science and Technology, Hiroshima University, Hiroshima 739-8528, Japan.
  • Barlowe C Department of Biochemistry, Geisel School of Medicine at Dartmouth, Hanover, NH 03755-3844, USA.
  • Riezman H Department of Biochemistry, University of Geneva, 1211 Geneva, Switzerland; Swiss National Centre for Competence in Research in Chemical Biology, 1211 Geneva, Switzerland. Electronic address: howard.riezman@unige.ch.
  • Roux A Department of Biochemistry, University of Geneva, 1211 Geneva, Switzerland; Swiss National Centre for Competence in Research in Chemical Biology, 1211 Geneva, Switzerland. Electronic address: aurelien.roux@unige.ch.
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  • 2018-06-12
Published in:
  • Current biology : CB. - 2018
COPII
budding assays
lysolipids
membrane curvature
membrane rigidity
phospholipase
vesicular transport
COP-Coated Vesicles
Lysophospholipids
Microsomes
Saccharomyces cerevisiae
English Coat protein complex II (COPII) proteins form vesicles from the endoplasmic reticulum to export cargo molecules to the Golgi apparatus. Among the many proteins involved in this process, Sec12 is a key regulator, functioning as the guanosine diphosphate (GDP) exchange factor for Sar1p, the small guanosine triphosphatase (GTPase) that initiates COPII assembly. Here we show that overexpression of phospholipase B3 in the thermosensitive sec12-4 mutant partially restores growth and protein transport at non-permissive temperatures. Lipidomics analyses of these cells show a higher content of lysophosphatidylinositol (lysoPI), consistent with the lipid specificity of PLB3. Furthermore, we show that lysoPI is specifically enriched in COPII vesicles isolated from in vitro budding assays. As these results suggested that lysophospholipids could facilitate budding under conditions of defective COPII coat dynamics, we reconstituted COPII binding onto giant liposomes with purified proteins and showed that lysoPI decreases membrane rigidity and enhances COPII recruitment to liposomes. Our results support a mechanical facilitation of COPII budding by lysophospholipids.
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  • English
Open access status
hybrid
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https://sonar.ch/global/documents/100688
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