The CORVET tethering complex interacts with the yeast Rab5 homolog Vps21 and is involved in endo-lysosomal biogenesis

Dev Cell. 2007 May;12(5):739-50. doi: 10.1016/j.devcel.2007.03.006.

Abstract

The dynamic equilibrium between vesicle fission and fusion at Golgi, endosome, and vacuole/lysosome is critical for the maintenance of organelle identity. It depends, among others, on Rab GTPases and tethering factors, whose function and regulation are still unclear. We now show that transport among Golgi, endosome, and vacuole is controlled by two homologous tethering complexes, the previously identified HOPS complex at the vacuole and a novel endosomal tethering (CORVET) complex, which interacts with the Rab GTPase Vps21. Both complexes share the four class C Vps proteins: Vps11, Vps16, Vps18, and Vps33. The HOPS complex, in addition, contains Vps41/Vam2 and Vam6, whereas the CORVET complex has the Vps41 homolog Vps8 and the (h)Vam6 homolog Vps3. Strikingly, the CORVET and HOPS complexes can interconvert; we identify two additional intermediate complexes, both consisting of the class C core bound to Vam6-Vps8 or Vps3-Vps41. Our data suggest that modular assembled tethering complexes define organelle biogenesis in the endocytic pathway.

MeSH terms

  • Endosomes / metabolism*
  • Lysosomes / metabolism*
  • Multiprotein Complexes / metabolism*
  • Mutation / genetics
  • Protein Binding
  • Saccharomyces cerevisiae / cytology
  • Saccharomyces cerevisiae / metabolism*
  • Saccharomyces cerevisiae Proteins / metabolism*
  • Sequence Homology, Amino Acid*
  • Vacuoles / metabolism
  • Vesicular Transport Proteins / metabolism
  • rab GTP-Binding Proteins / metabolism*
  • rab5 GTP-Binding Proteins / metabolism*

Substances

  • Multiprotein Complexes
  • Saccharomyces cerevisiae Proteins
  • VPS3 protein, S cerevisiae
  • VPS8 protein, S cerevisiae
  • Vesicular Transport Proteins
  • VPS21 protein, S cerevisiae
  • rab GTP-Binding Proteins
  • rab5 GTP-Binding Proteins