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Snc1p v‐SNARE Transport to the Prospore Membrane During Yeast Sporulation is Dependent on Endosomal Retrieval Pathways
Author(s) -
Morishita Masayo,
Mendonsa Rima,
Wright Jennifer,
Engebrecht JoAnne
Publication year - 2007
Publication title -
traffic
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.677
H-Index - 130
eISSN - 1600-0854
pISSN - 1398-9219
DOI - 10.1111/j.1600-0854.2007.00606.x
Subject(s) - endosome , retromer , microbiology and biotechnology , biology , golgi apparatus , vesicular transport proteins , vesicle , transport protein , vesicular transport protein , mutant , saccharomyces cerevisiae , yeast , biochemistry , membrane , vacuolar protein sorting , gene , endoplasmic reticulum , intracellular
Vesicular traffic is essential for sporulation in Saccharomyces cerevisiae . The Golgi‐associated retrograde protein (GARP) tethering complex is required for retrograde traffic from both the early and late endosomes to the Golgi. Analyses of GARP complex mutants in sporulation reveal defects in meiotic progression and spore formation. In contrast, inactivation of the retromer complex, which mediates vesicle budding and cargo selection from the late endosome, or Snx4p, which is involved in retrieval of proteins from the early endosome, has little effect on sporulation. A retromer GARP double mutant is defective in the formation of the prospore membrane (PSM) that surrounds the haploid nuclei. In the retromer GARP double mutant, PSM precursor vesicles carrying the cargo, Dtr1p, are transported to the spindle pole body (SPB), where PSM formation is initiated. However, the v‐SNARE Snc1p is not transported to the SPB in the double mutant, suggesting that the defect in PSM formation is because of the failure to retrieve Snc1p, and perhaps other proteins, from the endosomal pathway. Taken together, these results indicate that retrograde trafficking from the endosome is essential for sporulation by retrieving molecules important for PSM and spore wall formation.