A role for phosphatidic acid in COPI vesicle fission yields insights into Golgi maintenance

Nat Cell Biol. 2008 Oct;10(10):1146-53. doi: 10.1038/ncb1774. Epub 2008 Sep 7.

Abstract

Proteins essential for vesicle formation by the Coat Protein I (COPI) complex are being identified, but less is known about the role of specific lipids. Brefeldin-A ADP-ribosylated substrate (BARS) functions in the fission step of COPI vesicle formation. Here, we show that BARS induces membrane curvature in cooperation with phosphatidic acid. This finding has allowed us to further delineate COPI vesicle fission into two sub-stages: 1) an earlier stage of bud-neck constriction, in which BARS and other COPI components are required, and 2) a later stage of bud-neck scission, in which phosphatidic acid generated by phospholipase D2 (PLD2) is also required. Moreover, in contrast to the disruption of the Golgi seen on perturbing the core COPI components (such as coatomer), inhibition of PLD2 causes milder disruptions, suggesting that such COPI components have additional roles in maintaining Golgi structure other than through COPI vesicle formation.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • COP-Coated Vesicles / enzymology
  • COP-Coated Vesicles / metabolism*
  • COP-Coated Vesicles / ultrastructure
  • COS Cells
  • Carrier Proteins / chemistry
  • Carrier Proteins / metabolism
  • Chlorocebus aethiops
  • Golgi Apparatus / enzymology
  • Golgi Apparatus / metabolism*
  • Golgi Apparatus / ultrastructure
  • HeLa Cells
  • Humans
  • Intracellular Membranes / metabolism
  • Liposomes / metabolism
  • Mice
  • Phosphatidic Acids / metabolism*
  • Phospholipase D / metabolism
  • Protein Structure, Tertiary

Substances

  • Carrier Proteins
  • Liposomes
  • Phosphatidic Acids
  • phospholipase D2
  • Phospholipase D