A new type of coated vesicular carrier that appears not to contain clathrin: its possible role in protein transport within the Golgi stack

Cell. 1986 Jul 18;46(2):171-84. doi: 10.1016/0092-8674(86)90734-8.


Isolated Golgi membranes incubated in the presence of ATP and a cytosolic protein fraction form a population of coated buds or vesicles from the Golgi cisternae. The coats do not have the characteristic hexagonal-pentagonal basketwork of clathrin, and do not react with anti-clathrin polyclonal antibody. The conditions that produce these apparently nonclathrin-coated buds also reconstitute protein transport between compartments of the Golgi stack. The membrane of the buds contains the glycoprotein in transit through these Golgi stacks (VSV-encoded G protein). This suggests that protein transport through the Golgi stack is mediated by a new type of coated vesicle that does not contain clathrin. The concentration of G protein in the coated buds reflects the local concentration of G protein in the cisternae, raising the possibility that the Golgi coated vesicles may be "bulk" membrane carriers.

Publication types

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

MeSH terms

  • Animals
  • Biological Transport
  • Carrier Proteins / metabolism*
  • Clathrin / physiology*
  • Coated Pits, Cell-Membrane / metabolism*
  • Coated Pits, Cell-Membrane / ultrastructure
  • Cricetinae
  • Cricetulus
  • Endosomes / metabolism*
  • Female
  • Golgi Apparatus / metabolism*
  • Golgi Apparatus / physiology
  • Golgi Apparatus / ultrastructure
  • Membrane Glycoproteins*
  • Ovary
  • Vesicular stomatitis Indiana virus / metabolism
  • Viral Envelope Proteins*
  • Viral Proteins / metabolism


  • Carrier Proteins
  • Clathrin
  • G protein, vesicular stomatitis virus
  • Membrane Glycoproteins
  • Viral Envelope Proteins
  • Viral Proteins