Open AccessThe Saccharomyces cerevisiae protein Ccz1p interacts with components of the endosomal fusion machinery
Author(s) -
Kucharczyk Róża,
HoffmanSommer Marta,
Piekarska Iga,
Von Mollard Gabriele Fischer,
Rytka Joanna
Publication year - 2009
Publication title -
fems yeast research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.991
H-Index - 92
eISSN - 1567-1364
pISSN - 1567-1356
DOI - 10.1111/j.1567-1364.2009.00515.x
Subject(s) - endosome , biology , microbiology and biotechnology , vacuole , saccharomyces cerevisiae , biogenesis , lipid bilayer fusion , transport protein , protein targeting , gtpase , fusion protein , golgi apparatus , yeast , vesicular transport protein , vesicular transport proteins , phenotype , small gtpase , gene , membrane protein , biochemistry , vesicle , vacuolar protein sorting , cytoplasm , signal transduction , membrane , recombinant dna , endoplasmic reticulum , intracellular
The yeast protein Ccz1p is necessary for vacuolar protein trafficking and biogenesis. In a complex with Mon1p, it mediates fusion of transport intermediates with the vacuole membrane by activating the small GTPase Ypt7p. Additionally, genetic data suggest a role of Ccz1p in earlier transport steps, in the Golgi. In a search for further proteins interacting with Ccz1p, we identified the endosomal soluble N ‐ethylmaleimide‐sensitive factor attachment protein receptor Pep12p as an interaction partner of Ccz1p. Combining the ccz1 Δ mutation with deletions of PEP12 or other genes encoding components of the endosomal fusion machinery, VPS21, VPS9 or VPS45 , results in synthetic growth phenotypes. The genes MON1 and YPT7 also interact genetically with PEP12 . These results suggest that the Ccz1p–Mon1p–Ypt7p complex is involved in fusion of transport vesicles to multiple target membranes in yeast cells.