• Open Access

Sequential Depletion and Acquisition of Proteins during Golgi Stack Disassembly and Reformation

Authors

  • Jennifer Schoberer,

    1. Department of Applied Genetics and Cell Biology, University of Natural Resources and Applied Life Sciences, Vienna, Muthgasse 18, 1190 Vienna, Austria
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  • John Runions,

    1. School of Life Sciences, Oxford Brookes University, Headington Campus, Gipsy Lane, Oxford OX3 0BP, UK
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  • Herta Steinkellner,

    1. Department of Applied Genetics and Cell Biology, University of Natural Resources and Applied Life Sciences, Vienna, Muthgasse 18, 1190 Vienna, Austria
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  • Richard Strasser,

    Corresponding author
    1. Department of Applied Genetics and Cell Biology, University of Natural Resources and Applied Life Sciences, Vienna, Muthgasse 18, 1190 Vienna, Austria
      Richard Strasser, richard.strasser@boku.ac.at and Chris Hawes, chawes@brookes.ac.uk
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  • Chris Hawes,

    Corresponding author
    1. School of Life Sciences, Oxford Brookes University, Headington Campus, Gipsy Lane, Oxford OX3 0BP, UK
      Richard Strasser, richard.strasser@boku.ac.at and Chris Hawes, chawes@brookes.ac.uk
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  • Anne Osterrieder

    1. School of Life Sciences, Oxford Brookes University, Headington Campus, Gipsy Lane, Oxford OX3 0BP, UK
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Richard Strasser, richard.strasser@boku.ac.at and Chris Hawes, chawes@brookes.ac.uk

Abstract

Herein, we report the stepwise transport of multiple plant Golgi membrane markers during disassembly of the Golgi apparatus in tobacco leaf epidermal cells in response to the induced expression of the GTP-locked Sar1p or Brefeldin A (BFA), and reassembly on BFA washout. The distribution of fluorescent Golgi-resident N-glycan processing enzymes and matrix proteins (golgins) with specific cistrans-Golgi sub-locations was followed by confocal microscopy during disassembly and reassembly. The first event during Golgi disassembly was the loss of trans-Golgi enzymes and golgins from Golgi membranes, followed by a sequential redistribution of medial and cis-Golgi enzymes into the endoplasmic reticulum (ER), whilst golgins were relocated to the ER or cytoplasm. This event was confirmed by fractionation and immuno-blotting. The sequential redistribution of Golgi components in a trans–cis sequence may highlight a novel retrograde trafficking pathway between the trans-Golgi and the ER in plants. Release of Golgi markers from the ER upon BFA washout occurred in the opposite sequence, with cis-matrix proteins labelling Golgi-like structures before cis/medial enzymes. Trans-enzyme location was preceded by trans-matrix proteins being recruited back to Golgi membranes. Our results show that Golgi disassembly and reassembly occur in a highly ordered fashion in plants.

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