A role for BARS at the fission step of COPI vesicle formation from Golgi membrane

EMBO J. 2005 Dec 7;24(23):4133-43. doi: 10.1038/sj.emboj.7600873. Epub 2005 Nov 17.

Abstract

The core complex of Coat Protein I (COPI), known as coatomer, is sufficient to induce coated vesicular-like structures from liposomal membrane. In the context of biological Golgi membrane, both palmitoyl-coenzyme A (p-coA) and ARFGAP1, a GTPase-activating protein (GAP) for ADP-Ribosylation Factor 1, also participate in vesicle formation, but how their roles may be linked remains unknown. Moreover, whether COPI vesicle formation from Golgi membrane requires additional factors also remains unclear. We now show that Brefeldin-A ADP-Ribosylated Substrate (BARS) plays a critical role in the fission step of COPI vesicle formation from Golgi membrane. This role of BARS requires its interaction with ARFGAP1, which is in turn regulated oppositely by p-coA and nicotinamide adenine dinucleotide, which act as cofactors of BARS. Our findings not only identify a new factor needed for COPI vesicle formation from Golgi membrane but also reveal a surprising mechanism by which the roles of p-coA and GAP are linked in this process.

Publication types

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

MeSH terms

  • Acyltransferases / physiology
  • Alcohol Oxidoreductases
  • Animals
  • COS Cells
  • Chlorocebus aethiops
  • Coat Protein Complex I / metabolism*
  • Cytoplasmic Vesicles / metabolism*
  • Cytoplasmic Vesicles / ultrastructure
  • DNA-Binding Proteins / physiology*
  • GTPase-Activating Proteins / metabolism
  • Golgi Apparatus / physiology*
  • Golgi Apparatus / ultrastructure
  • Humans
  • Mutation
  • NAD / physiology
  • Palmitoyl Coenzyme A / physiology
  • Phosphoproteins / physiology*

Substances

  • Coat Protein Complex I
  • DNA-Binding Proteins
  • GTPase-Activating Proteins
  • Phosphoproteins
  • NAD
  • Palmitoyl Coenzyme A
  • Alcohol Oxidoreductases
  • C-terminal binding protein
  • Acyltransferases