Journal
MOLECULAR BIOLOGY OF THE CELL
Volume 22, Issue 14, Pages 2564-2578Publisher
AMER SOC CELL BIOLOGY
DOI: 10.1091/mbc.E10-06-0493
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Funding
- Max Planck Society
- Deutsche Forschungsgemeinschaft [Z.W. 71/2-1, 3-1]
- European Commission
- Gottingen Graduate School for Neurosciences and Molecular Biosciences
- Helen Hay Whitney Foundation
- National Institutes of Health [K99 MH082109]
- University Medical Faculty Gottingen
- Max-Planck Society
- European Union coordination action Network of European Neuroscience Institutes
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In yeast the Golgi-associated retrograde protein (GARP) complex is required for tethering of endosome-derived transport vesicles to the late Golgi. It consists of four subunits-Vps51p, Vps52p, Vps53p, and Vps54p-and shares similarities with other multimeric tethering complexes, such as the conserved oligomeric Golgi (COG) and the exocyst complex. Here we report the functional characterization of the GARP complex in the nematode Caenorhabditis elegans. Furthermore, we identified the C. elegans Vps51 subunit, which is conserved in all eukaryotes. GARP mutants are viable but show lysosomal defects. We show that GARP subunits bind specific sets of Golgi SNAREs within the yeast two-hybrid system. This suggests that the C. elegans GARP complex also facilitates tethering as well as SNARE complex assembly at the Golgi. The GARP and COG tethering complexes may have overlapping functions for retrograde endosome-to-Golgi retrieval, since loss of both complexes leads to a synthetic lethal phenotype.
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