Coat proteins regulating membrane traffic

Int Rev Cytol. 2000;195:67-144. doi: 10.1016/s0074-7696(08)62704-7.


This review focuses on the roles of coat proteins in regulating the membrane traffic of eukaryotic cells. Coat proteins are recruited to the donor organelle membrane from a cytosolic pool by specific small GTP-binding proteins and are required for the budding of coated vesicles. This review first describes the four types of coat complexes that have been characterized so far: clathrin and its adaptors, the adaptor-related AP-3 complex, COPI, and COPII. It then discusses the ascribed functions of coat proteins in vesicular transport, including the physical deformation of the membrane into a bud, the selection of cargo, and the targeting of the budded vesicle. It also mentions how the coat proteins may function in an alternative model for transport, namely via tubular connections, and how traffic is regulated. Finally, this review outlines the evidence that related coat proteins may regulate other steps of membrane traffic.

Publication types

  • Review

MeSH terms

  • Adaptor Protein Complex alpha Subunits
  • Adaptor Proteins, Vesicular Transport
  • Animals
  • Biological Transport
  • Bodily Secretions
  • Capsid / metabolism*
  • Carrier Proteins / metabolism
  • Carrier Proteins / physiology
  • Cell Membrane / metabolism
  • Clathrin / metabolism
  • Coat Protein Complex I / metabolism
  • Coated Vesicles / metabolism*
  • Endocytosis
  • Membrane Proteins / metabolism
  • Membrane Proteins / physiology
  • Monomeric Clathrin Assembly Proteins*


  • Adaptor Protein Complex alpha Subunits
  • Adaptor Proteins, Vesicular Transport
  • Carrier Proteins
  • Clathrin
  • Coat Protein Complex I
  • Membrane Proteins
  • Monomeric Clathrin Assembly Proteins
  • clathrin assembly protein AP180