title: Evidence for prebudding arrest of ER export in animal cell mitosis and its role in generating Golgi partitioning intermediates.
abstract: During mitosis the interconnected Golgi complex of animal cells breaks down to produce both finely dispersed elements and discrete vesiculotubular structures. The endoplasmic reticulum (ER) plays a controversial role in generating these partitioning intermediates and here we highlight the importance of mitotic ER export arrest in this process. We show that experimental inhibition of ER export (by microinjecting dominant negative Sar1 mutant proteins) is sufficient to induce and maintain transformation of Golgi cisternae to vesiculotubular remnants during interphase and telophase, respectively. We also show that buds on the ER, ER exit sites and COPII vesicles are markedly depleted in mitotic cells and COPII components Sec23p, Sec24p, Sec13p and Sec31p redistribute into the cytosol, indicating ER export is inhibited at an early stage. Finally, we find a markedly uneven distribution of Golgi residents over residual exit sites of metaphase cells, consistent with tubulovesicular Golgi remnants arising by fragmentation rather than redistribution via the ER. Together, these results suggest selective recycling of Golgi residents, combined with prebudding cessation of ER export, induces transformation of Golgi cisternae to vesiculotubular remnants in mitotic cells. The vesiculotubular Golgi remnants, containing populations of slow or nonrecycling Golgi components, arise by fragmentation of a depleted Golgi ribbon independently from the ER.
authors.affiliation: School of Life Sciences, WTB/MSI Complex, University of Dundee, Dundee DD1 5EH, UK.
authors.forename: A R
authors.initials: AR
authors.lastname: Prescott
authors.forename: T
authors.initials: T
authors.lastname: Farmaki
authors.forename: C
authors.initials: C
authors.lastname: Thomson
authors.forename: J
authors.initials: J
authors.lastname: James
authors.forename: J P
authors.initials: JP
authors.lastname: Paccaud
authors.forename: B L
authors.initials: BL
authors.lastname: Tang
authors.forename: W
authors.initials: W
authors.lastname: Hong
authors.forename: M
authors.initials: M
authors.lastname: Quinn
authors.forename: S
authors.initials: S
authors.lastname: Ponnambalam
authors.forename: J
authors.initials: J
authors.lastname: Lucocq
mesh_terms: D022181:COP-Coated Vesicles; D004721:Endoplasmic Reticulum / Q000502:physiology* / Q000648:ultrastructure; D006056:Golgi Apparatus / Q000502:physiology*; D006153:Guanosine Diphosphate / Q000502:physiology; D006160:Guanosine Triphosphate / Q000502:physiology; D006367:HeLa Cells; D006801:Humans; D008845:Microinjections; D008854:Microscopy, Electron; D008856:Microscopy, Fluorescence; D008938:Mitosis / Q000502:physiology*; D020559:Monomeric GTP-Binding Proteins / Q000008:administration & dosage / Q000235:genetics / Q000494:pharmacology; D009154:Mutation; D029701:Saccharomyces cerevisiae Proteins; D033921:Vesicular Transport Proteins
chemical_list: D029701:Saccharomyces cerevisiae Proteins; D033921:Vesicular Transport Proteins; D006153:Guanosine Diphosphate; D006160:Guanosine Triphosphate; D020559:Monomeric GTP-Binding Proteins; C077395:SAR1 protein, S cerevisiae