title: Yeast-to-hyphal transition triggers formin-dependent Golgi localization to the growing tip in Candida albicans.
abstract: Rapid and long-distance secretion of membrane components is critical for hyphal formation in filamentous fungi, but the mechanisms responsible for polarized trafficking are not well understood. Here, we demonstrate that in Candida albicans, the majority of the Golgi complex is redistributed to the distal region during hyphal formation. Randomly distributed Golgi puncta in yeast cells cluster toward the growing tip during hyphal formation, remain associated with the distal portion of the filament during its extension, and are almost absent from the cell body. This restricted Golgi localization pattern is distinct from other organelles, including the endoplasmic reticulum, vacuole and mitochondria, which remain distributed throughout the cell body and hypha. Hyphal-induced positioning of the Golgi and the maintenance of its structural integrity requires actin cytoskeleton, but not microtubules. Absence of the formin Bni1 causes a hyphal-specific dispersal of the Golgi into a haze of finely dispersed vesicles with a sedimentation density no different from that of normal Golgi. These results demonstrate the existence of a hyphal-specific, Bni1-dependent cue for Golgi integrity and positioning at the distal portion of the hyphal tip, and suggest that filamentous fungi have evolved a novel strategy for polarized secretion, involving a redistribution of the Golgi to the growing tip.
authors.affiliation: Department of Biochemistry and Cell Biology, Stony Brook University, Stony Brook, NY 11794-5215, USA.
authors.forename: Padmashree C G
authors.initials: PC
authors.lastname: Rida
authors.forename: Akiko
authors.initials: A
authors.lastname: Nishikawa
authors.forename: Gena Y
authors.initials: GY
authors.lastname: Won
authors.forename: Neta
authors.initials: N
authors.lastname: Dean
mesh_terms: D000199:Actins / Q000502:physiology; D002176:Candida albicans / Q000254:growth & development*; D016764:Cell Polarity; D002478:Cells, Cultured; D004721:Endoplasmic Reticulum / Q000378:metabolism; D000939:Epitopes / Q000235:genetics; D005455:Fluorescent Antibody Technique; D005656:Fungal Proteins / Q000235:genetics / Q000378:metabolism* / Q000502:physiology; D017930:Genes, Reporter / Q000235:genetics; D006056:Golgi Apparatus / Q000378:metabolism* / Q000648:ultrastructure; D025301:Hyphae / Q000254:growth & development* / Q000378:metabolism; D008840:Microfilament Proteins / Q000235:genetics / Q000378:metabolism* / Q000502:physiology; D008870:Microtubules / Q000502:physiology; D008954:Models, Biological; D029701:Saccharomyces cerevisiae Proteins / Q000235:genetics / Q000378:metabolism* / Q000502:physiology; D015398:Signal Transduction; D014617:Vacuoles / Q000378:metabolism; D015003:Yeasts / Q000254:growth & development*
chemical_list: D000199:Actins; C105191:Bni1 protein, S cerevisiae; D000939:Epitopes; D005656:Fungal Proteins; D008840:Microfilament Proteins; D029701:Saccharomyces cerevisiae Proteins