A coat subunit of Golgi-derived non-clathrin-coated vesicles with homology to the clathrin-coated vesicle coat protein beta-adaptin

Nature. 1991 Jan 17;349(6306):215-20. doi: 10.1038/349215a0.


Four high-molecular-weight proteins form the main subunits of the coat of Golgi-derived (non-clathrin) coated vesicles. One of these coat proteins, beta-COP, is identical to a Golgi-associated protein of relative mass 110,000 (110K) that shares homology with the adaptin proteins of clathrin-coated vesicles. This connection, and the comparable molecular weights of the coat proteins of Golgi-derived and clathrin-coated vesicles, indicates that they may be structurally related. The identification of beta-COP as the 110K protein explains the blocking of secretion by the drug brefeldin A.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Adaptor Protein Complex beta Subunits
  • Amino Acid Sequence
  • Animals
  • Cell Fractionation / methods
  • Clathrin / chemistry*
  • Coated Pits, Cell-Membrane / chemistry*
  • Coated Pits, Cell-Membrane / ultrastructure
  • Golgi Apparatus / chemistry*
  • Membrane Proteins / chemistry*
  • Membrane Proteins / isolation & purification
  • Microscopy, Immunoelectron
  • Molecular Sequence Data
  • Proteins / chemistry*
  • Proteins / isolation & purification
  • Sequence Homology, Nucleic Acid


  • Adaptor Protein Complex beta Subunits
  • Clathrin
  • Membrane Proteins
  • Proteins