title: Snc1p v-SNARE transport to the prospore membrane during yeast sporulation is dependent on endosomal retrieval pathways.
abstract: 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.
authors.affiliation: Section of Molecular and Cellular Biology, University of California, Davis, Davis, CA 95616, USA.
authors.forename: Masayo
authors.initials: M
authors.lastname: Morishita
authors.forename: Rima
authors.initials: R
authors.lastname: Mendonsa
authors.forename: Jennifer
authors.initials: J
authors.lastname: Wright
authors.forename: Joanne
authors.initials: J
authors.lastname: Engebrecht
mesh_terms: D002352:Carrier Proteins / Q000235:genetics / Q000378:metabolism; D002462:Cell Membrane / Q000378:metabolism; D002473:Cell Wall / Q000378:metabolism; D002687:Chitin Synthase; D019926:Cyclin B / Q000235:genetics / Q000378:metabolism; D011992:Endosomes / Q000378:metabolism*; D005964:Glucosyltransferases / Q000235:genetics / Q000378:metabolism; D006056:Golgi Apparatus / Q000378:metabolism; D049452:Green Fluorescent Proteins / Q000235:genetics / Q000378:metabolism; D007425:Intracellular Membranes / Q000378:metabolism; D008540:Meiosis / Q000235:genetics; D008565:Membrane Proteins / Q000235:genetics / Q000378:metabolism; D026901:Membrane Transport Proteins / Q000235:genetics / Q000378:metabolism; D046529:Microscopy, Electron, Transmission; D008954:Models, Biological; D009154:Mutation; D021381:Protein Transport / Q000502:physiology; D050683:R-SNARE Proteins / Q000235:genetics / Q000378:metabolism*; D011993:Recombinant Fusion Proteins / Q000235:genetics / Q000378:metabolism; D050600:SNARE Proteins / Q000235:genetics / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000235:genetics / Q000378:metabolism / Q000502:physiology*; D029701:Saccharomyces cerevisiae Proteins / Q000235:genetics / Q000378:metabolism*; D013172:Spores, Fungal / Q000254:growth & development* / Q000378:metabolism / Q000648:ultrastructure; D033921:Vesicular Transport Proteins / Q000235:genetics / Q000378:metabolism
chemical_list: C093749:CLB2 protein, S cerevisiae; D002352:Carrier Proteins; D019926:Cyclin B; C470564:Dtr1 protein, S cerevisiae; D008565:Membrane Proteins; D026901:Membrane Transport Proteins; D050683:R-SNARE Proteins; D011993:Recombinant Fusion Proteins; D050600:SNARE Proteins; C083241:SNC1 protein, S cerevisiae; D029701:Saccharomyces cerevisiae Proteins; C078863:VPS17 protein, S cerevisiae; C093602:VPS52 protein, S cerevisiae; C492177:VPS53 protein, S cerevisiae; C117606:VPS54 protein, S cerevisiae; D033921:Vesicular Transport Proteins; D049452:Green Fluorescent Proteins; D005964:Glucosyltransferases; C069390:CHS3 protein, S cerevisiae; D002687:Chitin Synthase; C095724:GSC2 protein, S cerevisiae