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The CORVET subunit Vps8 cooperates with the Rab5 homolog Vps21 to induce clustering of late endosomal compartments.
Results suggest that the CORVET complex is built of subunits with distinct activities and potentially, their sequential assembly could regulate tethering and successive fusion at the late endosomes.
Functional Separation of Endosomal Fusion Factors and the Class C Core Vacuole/Endosome Tethering (CORVET) Complex in Endosome Biogenesis*
- Margarita Cabrera, H. Arlt, C. Ungermann
- Biology, ChemistryThe Journal of Biological Chemistry
- 22 December 2012
This study reveals a unique role of CORVET in the sorting of biosynthetic cargo to the vacuole/lysosome and uncovers that Muk1 can compensate for loss of Vps9 in CORVet localization, indicating that two Rab5 guanine nucleotide exchange factors operate in the endocytic pathway.
Membrane dynamics and fusion at late endosomes and vacuoles--Rab regulation, multisubunit tethering complexes and SNAREs.
The N-Terminal Domains of Vps3 and Vps8 Are Critical for Localization and Function of the CORVET Tethering Complex on Endosomes
It is shown that the CORVET-specific Vps3 and Vps8 subunits, which interact with Rab5/Vps21, require their N-terminal domains for localization and function and has beyond its putative β-propeller domains additional binding sites for endosomes, which could be important to bind Vps21 and other endosome-specific factors for efficient endosomal tethering.
1 FUNCTIONAL SEPARATION OF ENDOSOMAL FUSION FACTORS AND THE CORVET TETHERING COMPLEX IN ENDOSOME BIOGENESIS
The data reveal a unique role of CORVET in sorting of biosynthetic cargo to the vacuole, and show that it acts independently of the Vac1 tether, and requires activated Rab5 homologs for localization.