title: Organization and dynamics of the Aspergillus nidulans Golgi during apical extension and mitosis.
abstract: Aspergillus nidulans hyphae grow exclusively by apical extension. Golgi equivalents (GEs) labeled with mRFP-tagged PH(OSBP) domain form a markedly polarized, dynamic network of ring-shaped and fenestrated cisternae that remains intact during "closed" mitosis. mRFP-PH(OSBP) GEs advance associated with the growing apex where secretion predominates but do not undergo long-distance movement toward the tip that could account for their polarization. mRFP-PH(OSBP) GEs overlap with the trans-Golgi resident Sec7 but do not colocalize with also polarized accretions of the early Golgi marker GrhA(Grh1)-GFP, indicating that early and late Golgi membranes segregate spatially. AnSec23-GFP ER exit sites (ERES) are numerous, relatively static foci localizing across the entire cell. However, their density is greatest near the tip, correlating with predominance of early and trans-Golgi elements in this region. Whereas GrhA-GFP structures and ERES reach the apical dome, mRFP-PH(OSBP) GEs are excluded from this region, which contains the endosome dynein loading zone. After latrunculin-mediated F-actin disruption, mRFP-PH(OSBP) GEs fragment and, like AnSec23-GFP ERES, depolarize. Brefeldin A transiently collapses late and early GEs into distinct aggregates containing Sec7/mRFP-PH(OSBP) and GrhA-GFP, respectively, temporarily arresting apical extension. Rapid growth reinitiates after washout, correlating with reacquisition of the normal Golgi organization that, we conclude, is required for apical extension.
authors.affiliation: Departamento de Microbiología Molecular, Centro de Investigaciones Biológicas C.S.I.C., Madrid 28040, Spain.
authors.forename: Areti
authors.initials: A
authors.lastname: Pantazopoulou
authors.forename: Miguel A
authors.initials: MA
authors.lastname: Peñalva
mesh_terms: D000818:Animals; D001233:Aspergillus nidulans / Q000187:drug effects / Q000254:growth & development* / Q000648:ultrastructure; D020126:Brefeldin A / Q000494:pharmacology; D019086:Bridged Bicyclo Compounds, Heterocyclic / Q000494:pharmacology; D016764:Cell Polarity; D048430:Cell Shape / Q000187:drug effects; D005656:Fungal Proteins / Q000235:genetics / Q000502:physiology; D017930:Genes, Reporter; D005813:Genes, Synthetic; D006056:Golgi Apparatus / Q000648:ultrastructure*; D006801:Humans; D025301:Hyphae / Q000187:drug effects / Q000254:growth & development* / Q000648:ultrastructure; D007091:Image Processing, Computer-Assisted; D007425:Intracellular Membranes / Q000648:ultrastructure; D008856:Microscopy, Fluorescence; D008938:Mitosis; D015388:Organelles / Q000737:chemistry / Q000648:ultrastructure; D018129:Phosphatidylinositol Phosphates / Q000032:analysis / Q000502:physiology; D017434:Protein Structure, Tertiary; D051381:Rats; D011987:Receptors, Steroid / Q000032:analysis / Q000737:chemistry / Q000235:genetics; D011993:Recombinant Fusion Proteins / Q000032:analysis / Q000737:chemistry; D053778:Thiazolidines / Q000494:pharmacology; D010738:Type C Phospholipases / Q000032:analysis / Q000737:chemistry / Q000235:genetics; D000098825:Oxysterol Binding Proteins
chemical_list: D019086:Bridged Bicyclo Compounds, Heterocyclic; D005656:Fungal Proteins; D018129:Phosphatidylinositol Phosphates; D011987:Receptors, Steroid; D011993:Recombinant Fusion Proteins; D053778:Thiazolidines; D000098825:Oxysterol Binding Proteins; C037178:phosphatidylinositol 4-phosphate; D020126:Brefeldin A; D010738:Type C Phospholipases; C432456:phospholipase C1; C037068:latrunculin B
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