title: Golgi membranes are absorbed into and reemerge from the ER during mitosis.
abstract: Quantitative imaging and photobleaching were used to measure ER/Golgi recycling of GFP-tagged Golgi proteins in interphase cells and to monitor the dissolution and reformation of the Golgi during mitosis. In interphase, recycling occurred every 1.5 hr, and blocking ER egress trapped cycling Golgi enzymes in the ER with loss of Golgi structure. In mitosis, when ER export stops, Golgi proteins redistributed into the ER as shown by quantitative imaging in vivo and immuno-EM. Comparison of the mobilities of Golgi proteins and lipids ruled out the persistence of a separate mitotic Golgi vesicle population and supported the idea that all Golgi components are absorbed into the ER. Moreover, reassembly of the Golgi complex after mitosis failed to occur when ER export was blocked. These results demonstrate that in mitosis the Golgi disperses and reforms through the intermediary of the ER, exploiting constitutive recycling pathways. They thus define a novel paradigm for Golgi genesis and inheritance.
authors.affiliation: Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, National Istitutes of Health, Bethesda, Maryland 20892-5430, USA.
authors.forename: K J
authors.initials: KJ
authors.lastname: Zaal
authors.forename: C L
authors.initials: CL
authors.lastname: Smith
authors.forename: R S
authors.initials: RS
authors.lastname: Polishchuk
authors.forename: N
authors.initials: N
authors.lastname: Altan
authors.forename: N B
authors.initials: NB
authors.lastname: Cole
authors.forename: J
authors.initials: J
authors.lastname: Ellenberg
authors.forename: K
authors.initials: K
authors.lastname: Hirschberg
authors.forename: J F
authors.initials: JF
authors.lastname: Presley
authors.forename: T H
authors.initials: TH
authors.lastname: Roberts
authors.forename: E
authors.initials: E
authors.lastname: Siggia
authors.forename: R D
authors.initials: RD
authors.lastname: Phair
authors.forename: J
authors.initials: J
authors.lastname: Lippincott-Schwartz
mesh_terms: D000818:Animals; D002460:Cell Line; D016207:Cytokines / Q000378:metabolism; D004721:Endoplasmic Reticulum / Q000378:metabolism* / Q000648:ultrastructure; D005455:Fluorescent Antibody Technique; D005700:Galactosyltransferases / Q000235:genetics; D006056:Golgi Apparatus / Q000378:metabolism* / Q000648:ultrastructure; D049452:Green Fluorescent Proteins; D006801:Humans; D007399:Interphase / Q000502:physiology; D007425:Intracellular Membranes / Q000378:metabolism; D008164:Luminescent Proteins / Q000235:genetics; D008677:Metaphase / Q000502:physiology; D008854:Microscopy, Electron; D008938:Mitosis / Q000502:physiology*; D020559:Monomeric GTP-Binding Proteins / Q000378:metabolism; D011993:Recombinant Fusion Proteins / Q000235:genetics / Q000378:metabolism; D029701:Saccharomyces cerevisiae Proteins; D033921:Vesicular Transport Proteins
chemical_list: D016207:Cytokines; D008164:Luminescent Proteins; D011993:Recombinant Fusion Proteins; D029701:Saccharomyces cerevisiae Proteins; D033921:Vesicular Transport Proteins; D049452:Green Fluorescent Proteins; D005700:Galactosyltransferases; D020559:Monomeric GTP-Binding Proteins; C077395:SAR1 protein, S cerevisiae