title: Golgi clusters and vesicles mediate mitotic inheritance independently of the endoplasmic reticulum.
abstract: We have examined the fate of Golgi membranes during mitotic inheritance in animal cells using four-dimensional fluorescence microscopy, serial section reconstruction of electron micrographs, and peroxidase cytochemistry to track the fate of a Golgi enzyme fused to horseradish peroxidase. All three approaches show that partitioning of Golgi membranes is mediated by Golgi clusters that persist throughout mitosis, together with shed vesicles that are often found associated with spindle microtubules. We have been unable to find evidence that Golgi membranes fuse during the later phases of mitosis with the endoplasmic reticulum (ER) as a strategy for Golgi partitioning (Zaal, K.J., C.L. Smith, R.S. Polishchuk, N. Altan, N.B. Cole, J. Ellenberg, K. Hirschberg, J.F. Presley, T.H. Roberts, E. Siggia, et al. 1999. Cell. 99:589-601) and suggest that these results, in part, are the consequence of slow or abortive folding of GFP-Golgi chimeras in the ER. Furthermore, we show that accurate partitioning is accomplished early in mitosis, by a process of cytoplasmic redistribution of Golgi fragments and vesicles yielding a balance of Golgi membranes on either side of the metaphase plate before cell division.
authors.affiliation: Institute of Biotechnology, Electron Microscopy Unit, University of Helsinki, 00014 Helsinki, Finland.
authors.forename: E
authors.initials: E
authors.lastname: Jokitalo
authors.forename: N
authors.initials: N
authors.lastname: Cabrera-Poch
authors.forename: G
authors.initials: G
authors.lastname: Warren
authors.forename: D T
authors.initials: DT
authors.lastname: Shima
mesh_terms: D000818:Animals; D002460:Cell Line; D006224:Cricetinae; D022162:Cytoplasmic Vesicles / Q000378:metabolism* / Q000648:ultrastructure; D004721:Endoplasmic Reticulum / Q000378:metabolism* / Q000648:ultrastructure; D006056:Golgi Apparatus / Q000378:metabolism* / Q000648:ultrastructure; D006735:Horseradish Peroxidase / Q000235:genetics; D006801:Humans; D007425:Intracellular Membranes / Q000378:metabolism; D008677:Metaphase / Q000502:physiology; D008856:Microscopy, Fluorescence / Q000379:methods; D008870:Microtubules / Q000378:metabolism; D008938:Mitosis / Q000502:physiology*; D017351:N-Acetylglucosaminyltransferases / Q000235:genetics; D009237:N-Acetyllactosamine Synthase / Q000235:genetics; D051381:Rats; D011993:Recombinant Fusion Proteins / Q000235:genetics / Q000378:metabolism; D008941:Spindle Apparatus / Q000378:metabolism; D013692:Telophase / Q000502:physiology; D014162:Transfection
chemical_list: D011993:Recombinant Fusion Proteins; D006735:Horseradish Peroxidase; D017351:N-Acetylglucosaminyltransferases; C024850:alpha-1,3-mannosyl-glycoprotein beta-1,2-N-acetylglucosaminyltransferase I; D009237:N-Acetyllactosamine Synthase