title: cis-Golgi proteins accumulate near the ER exit sites and act as the scaffold for Golgi regeneration after brefeldin A treatment in tobacco BY-2 cells.
abstract: The Golgi apparatus forms stacks of cisternae in many eukaryotic cells. However, little is known about how such a stacked structure is formed and maintained. To address this question, plant cells provide a system suitable for live-imaging approaches because individual Golgi stacks are well separated in the cytoplasm. We established tobacco BY-2 cell lines expressing multiple Golgi markers tagged by different fluorescent proteins and observed their responses to brefeldin A (BFA) treatment and BFA removal. BFA treatment disrupted cis, medial, and trans cisternae but caused distinct relocalization patterns depending on the proteins examined. Medial- and trans-Golgi proteins, as well as one cis-Golgi protein, were absorbed into the endoplasmic reticulum (ER), but two other cis-Golgi proteins formed small punctate structures. After BFA removal, these puncta coalesced first, and then the Golgi stacks regenerated from them in the cis-to-trans order. We suggest that these structures have a property similar to the ER-Golgi intermediate compartment and function as the scaffold of Golgi regeneration.
authors: Department of Biological Sciences, Graduate School of Science, University of Tokyo, Tokyo, Japan.
authors: Yoko
authors: Y
authors: Ito
authors: Tomohiro
authors: T
authors: Uemura
authors: Keiko
authors: K
authors: Shoda
authors: Masaru
authors: M
authors: Fujimoto
authors: Takashi
authors: T
authors: Ueda
authors: Akihiko
authors: A
authors: Nakano
mesh_terms: D008841:Actin Cytoskeleton / Q000378:metabolism; D001426:Bacterial Proteins / Q000378:metabolism; D020126:Brefeldin A / Q000494:pharmacology*; D002478:Cells, Cultured; D004721:Endoplasmic Reticulum / Q000187:drug effects / Q000378:metabolism* / Q000648:ultrastructure; D006056:Golgi Apparatus / Q000187:drug effects / Q000378:metabolism* / Q000648:ultrastructure; D049452:Green Fluorescent Proteins / Q000378:metabolism; D008164:Luminescent Proteins / Q000378:metabolism; D008565:Membrane Proteins / Q000378:metabolism; D008856:Microscopy, Fluorescence; D010940:Plant Proteins / Q000378:metabolism; D011500:Protein Synthesis Inhibitors / Q000494:pharmacology*; D021381:Protein Transport; D011993:Recombinant Fusion Proteins / Q000378:metabolism; D059008:Time-Lapse Imaging; D014026:Nicotiana / Q000166:cytology*
chemical_list: D001426:Bacterial Proteins; D008164:Luminescent Proteins; D008565:Membrane Proteins; D010940:Plant Proteins; D011500:Protein Synthesis Inhibitors; D011993:Recombinant Fusion Proteins; C054562:yellow fluorescent protein, Bacteria; D049452:Green Fluorescent Proteins; D020126:Brefeldin A