Transport according to GARP: receiving retrograde cargo at the trans-Golgi network

Trends Cell Biol. 2011 Mar;21(3):159-67. doi: 10.1016/j.tcb.2010.11.003. Epub 2010 Dec 21.


Tethering factors are large protein complexes that capture transport vesicles and enable their fusion with acceptor organelles at different stages of the endomembrane system. Recent studies have shed new light on the structure and function of a heterotetrameric tethering factor named Golgi-associated retrograde protein (GARP), which promotes fusion of endosome-derived, retrograde transport carriers to the trans-Golgi network (TGN). X-ray crystallography of the Vps53 and Vps54 subunits of GARP has revealed that this complex is structurally related to other tethering factors such as the exocyst, the conserved oligomeric Golgi (COG) and Dsl1 (dependence on SLY1-20) complexes, indicating that they all might work by a similar mechanism. Loss of GARP function compromises the growth, fertility and/or viability of the defective organisms, emphasizing the essential nature of GARP-mediated retrograde transport.

Publication types

  • Review

MeSH terms

  • Animals
  • Biological Transport
  • Carrier Proteins / chemistry
  • Carrier Proteins / metabolism*
  • GTP Phosphohydrolases / metabolism
  • Humans
  • SNARE Proteins / metabolism
  • Vesicular Transport Proteins / chemistry
  • Vesicular Transport Proteins / metabolism*
  • trans-Golgi Network / metabolism*


  • Carrier Proteins
  • SNARE Proteins
  • Vesicular Transport Proteins
  • GTP Phosphohydrolases