Vps-C complexes: gatekeepers of endolysosomal traffic

Curr Opin Cell Biol. 2009 Aug;21(4):543-51. doi: 10.1016/j.ceb.2009.05.007. Epub 2009 Jul 3.


Genetic studies in yeast, plants, insects, and mammals have identified four universally conserved proteins, together called Vps Class C, that are essential for late endosome and lysosome assembly and for numerous endolysosomal trafficking pathways, including the terminal stages of autophagy. Two Vps-C complexes, HOPS and CORVET, incorporate diverse biochemical functions: they tether membranes, stimulate Rab nucleotide exchange, guide SNARE assembly to drive membrane fusion, and possibly act as ubiquitin ligases. Recent studies offer new insight into the complex relationships between Vps-C complexes and their cognate Rab small GTP-binding (G-)proteins at endosomes and lysosomes. Accumulating evidence supports the view that Vps-C complexes implement a regulatory logic that governs endomembrane identity and dynamics.

Publication types

  • Research Support, N.I.H., Extramural
  • Review

MeSH terms

  • Autophagy
  • Endosomes / metabolism*
  • GTP-Binding Proteins / chemistry
  • Gene Expression Regulation, Fungal
  • Golgi Apparatus / metabolism
  • Lysosomes / chemistry
  • Lysosomes / metabolism*
  • Models, Biological
  • Mutation
  • Organelles / metabolism
  • Protein Transport
  • SNARE Proteins / chemistry
  • SNARE Proteins / metabolism*
  • Saccharomyces cerevisiae / metabolism
  • Saccharomyces cerevisiae Proteins / chemistry*
  • Ubiquitin / metabolism
  • Vesicular Transport Proteins / chemistry*
  • Vesicular Transport Proteins / physiology*


  • SNARE Proteins
  • Saccharomyces cerevisiae Proteins
  • Ubiquitin
  • Vesicular Transport Proteins
  • GTP-Binding Proteins