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

Autor(en): Peplowska, Karolina
Markgraf, Daniel F.
Ostrowicz, Clemens W.
Bange, Gert
Ungermann, Christian 
Stichwörter: Cell Biology; Developmental Biology; DOCKING; GUANINE-NUCLEOTIDE EXCHANGE; HOMOTYPIC VACUOLE FUSION; LATE ENDOSOMES; LATE GOLGI; ORGANELLE IDENTITY; RING FINGER PROTEIN; SACCHAROMYCES-CEREVISIAE; SNARE COMPLEX; TRANSPORT
Erscheinungsdatum: 2007
Herausgeber: CELL PRESS
Journal: DEVELOPMENTAL CELL
Volumen: 12
Ausgabe: 5
Startseite: 739
Seitenende: 750
Zusammenfassung: 
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 complexe 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.
ISSN: 15345807
DOI: 10.1016/j.devcel.2007.03.006

Show full item record

Page view(s)

1
Last Week
0
Last month
0
checked on Feb 26, 2024

Google ScholarTM

Check

Altmetric