Beta-COP, a 110 kd protein associated with non-clathrin-coated vesicles and the Golgi complex, shows homology to beta-adaptin

Cell. 1991 Feb 8;64(3):649-65. doi: 10.1016/0092-8674(91)90248-w.


We have cloned and sequenced beta-COP, a peripheral 110 kd Golgi membrane protein. beta-COP shows significant homology to beta-adaptin. It is present in a membrane-bound form and in a cytosolic complex of 13-14S, with a Stokes radius of approximately 10 nm and an estimated Mr of approximately 550,000. By immunofluorescence labeling, beta-COP is associated with the structures of the Golgi complex. Immunoelectron microscopy has localized beta-COP to non-clathrin-coated vesicles and cisternae of the Golgi complex. These coated vesicles accumulate in rat liver Golgi fractions treated with GTP gamma S and strongly label for beta-COP. Our data suggest that beta-COP is a component of a coat associated with vesicles and cisternae of the Golgi complex.

Publication types

  • Comparative Study

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Antibodies, Monoclonal
  • Base Sequence
  • Cloning, Molecular
  • Coatomer Protein
  • DNA / genetics
  • Golgi Apparatus / ultrastructure*
  • Humans
  • Immunohistochemistry
  • Intracellular Membranes / ultrastructure
  • Membrane Proteins / genetics*
  • Mice
  • Microtubule-Associated Proteins / genetics*
  • Molecular Sequence Data
  • Molecular Weight
  • Rats
  • Restriction Mapping
  • Solubility
  • Vero Cells


  • Antibodies, Monoclonal
  • Coatomer Protein
  • Membrane Proteins
  • Microtubule-Associated Proteins
  • DNA

Associated data

  • GENBANK/M59201
  • GENBANK/M63698
  • GENBANK/M63700
  • GENBANK/M63702
  • GENBANK/M63718
  • GENBANK/S63145
  • GENBANK/S63146
  • GENBANK/S63147
  • GENBANK/S63148
  • GENBANK/X57228