The BioGRID | PUBLICATION VIEW

	Dev. Cell May (2007); 12(5):739-50
The CORVET tethering complex interacts with the yeast Rab5 homolog Vps21 and is involved in endo-lysosomal biogenesis-
Peplowska K, Markgraf DF, Ostrowicz CW, Bange G, Ungermann C
University of Osnabruck, Department of Biology, Biochemistry Section, Barbarastrasse 13, 49076 Osnabruck, Germany-
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-
[PUBMED: 17488625]