title: Golgi structure correlates with transitional endoplasmic reticulum organization in Pichia pastoris and Saccharomyces cerevisiae.
abstract: Golgi stacks are often located near sites of "transitional ER" (tER), where COPII transport vesicles are produced. This juxtaposition may indicate that Golgi cisternae form at tER sites. To explore this idea, we examined two budding yeasts: Pichia pastoris, which has coherent Golgi stacks, and Saccharomyces cerevisiae, which has a dispersed Golgi. tER structures in the two yeasts were visualized using fusions between green fluorescent protein and COPII coat proteins. We also determined the localization of Sec12p, an ER membrane protein that initiates the COPII vesicle assembly pathway. In P. pastoris, Golgi stacks are adjacent to discrete tER sites that contain COPII coat proteins as well as Sec12p. This arrangement of the tER-Golgi system is independent of microtubules. In S. cerevisiae, COPII vesicles appear to be present throughout the cytoplasm and Sec12p is distributed throughout the ER, indicating that COPII vesicles bud from the entire ER network. We propose that P. pastoris has discrete tER sites and therefore generates coherent Golgi stacks, whereas S. cerevisiae has a delocalized tER and therefore generates a dispersed Golgi. These findings open the way for a molecular genetic analysis of tER sites.
authors: Department of Molecular Genetics and Cell Biology, The University of Chicago, Chicago, Illinois 60637, USA.
authors: O W
authors: OW
authors: Rossanese
authors: J
authors: J
authors: Soderholm
authors: B J
authors: BJ
authors: Bevis
authors: I B
authors: IB
authors: Sears
authors: J
authors: J
authors: O'Connor
authors: E K
authors: EK
authors: Williamson
authors: B S
authors: BS
authors: Glick
mesh_terms: D002352:Carrier Proteins / Q000235:genetics / Q000378:metabolism; D002453:Cell Cycle; D004721:Endoplasmic Reticulum / Q000648:ultrastructure*; D005656:Fungal Proteins / Q000378:metabolism; D017930:Genes, Reporter; D006056:Golgi Apparatus / Q000648:ultrastructure*; D049452:Green Fluorescent Proteins; D020662:Guanine Nucleotide Exchange Factors; D007425:Intracellular Membranes / Q000648:ultrastructure; D008164:Luminescent Proteins / Q000032:analysis / Q000235:genetics; D008562:Membrane Glycoproteins / Q000378:metabolism; D008854:Microscopy, Electron; D016253:Microscopy, Immunoelectron; D008870:Microtubules / Q000187:drug effects; D015739:Nocodazole / Q000494:pharmacology; D010750:Phosphoproteins / Q000235:genetics / Q000378:metabolism; D010843:Pichia / Q000648:ultrastructure*; D011993:Recombinant Fusion Proteins / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000648:ultrastructure*; D029701:Saccharomyces cerevisiae Proteins; D013045:Species Specificity; D033921:Vesicular Transport Proteins
chemical_list: D002352:Carrier Proteins; D005656:Fungal Proteins; D020662:Guanine Nucleotide Exchange Factors; D008164:Luminescent Proteins; D008562:Membrane Glycoproteins; D010750:Phosphoproteins; D011993:Recombinant Fusion Proteins; C071239:SEC12 protein, S cerevisiae; C106113:SEC31 protein, S cerevisiae; D029701:Saccharomyces cerevisiae Proteins; D033921:Vesicular Transport Proteins; D049452:Green Fluorescent Proteins; D015739:Nocodazole