Long coiled-coil proteins and membrane traffic

Biochim Biophys Acta. 2003 Aug 18;1641(2-3):71-85. doi: 10.1016/s0167-4889(03)00088-0.


Protein transport between organelles is mediated by vesicles which must accurately dock and fuse with appropriate compartments. Over the past several years a large number of long coiled-coil proteins have been identified on the Golgi and on endosomes, mostly as auto-antigens in autoimmune disorders. Based on their restricted intracellular distributions and their predicted rod-like structure, these proteins have been proposed to play a role in tethering vesicles to target organelles prior to fusion. However, such proteins may also play a structural role, for example as components of a Golgi matrix, or as scaffolds for the assembly of other factors important for fusion. This review will examine what is known about the function of these large coiled-coil proteins in membrane traffic.

Publication types

  • Review

MeSH terms

  • Animals
  • Cell Membrane / physiology*
  • Endoplasmic Reticulum / physiology
  • Endosomes / physiology
  • Golgi Apparatus / physiology
  • Humans
  • Membrane Transport Proteins / physiology*
  • Protein Transport


  • Membrane Transport Proteins