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Stacks off tracks: A role for the golgin AtCASP in plant endoplasmic reticulum – Golgi apparatus tethering

View ORCID ProfileAnne Osterrieder, View ORCID ProfileStan W Botchway, Andy Ward, View ORCID ProfileTijs Ketelaar, View ORCID ProfileNorbert de Ruijter, View ORCID ProfileChris Hawes
doi: https://doi.org/10.1101/115840
Anne Osterrieder
Department of Biological and Medical Sciences, Faculty of Health and Life Sciences, Oxford Brookes University, Gipsy Lane, Headington, Oxford, OX3 0AZ, UK
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  • For correspondence: a.Costerrieder@brookes.ac.uk Chawes@brookes.ac.uk
Stan W Botchway
Central Laser Facility, Science and Technology Facilities Council, Research Complex at Harwell, Didcot, Oxon OX11 0FA, UK
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Andy Ward
Central Laser Facility, Science and Technology Facilities Council, Research Complex at Harwell, Didcot, Oxon OX11 0FA, UK
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Tijs Ketelaar
Laboratory of Cell Biology, Wageningen University, Droevendaalsesteeg 1, 6708PB Wageningen, The Netherlands
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Norbert de Ruijter
Laboratory of Cell Biology, Wageningen University, Droevendaalsesteeg 1, 6708PB Wageningen, The Netherlands
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Chris Hawes
Department of Biological and Medical Sciences, Faculty of Health and Life Sciences, Oxford Brookes University, Gipsy Lane, Headington, Oxford, OX3 0AZ, UK
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  • For correspondence: a.Costerrieder@brookes.ac.uk Chawes@brookes.ac.uk
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Abstract

The plant Golgi apparatus modifies and sorts incoming proteins from the endoplasmic reticulum (ER), and synthesises cell wall matrix material. Plant cells possess numerous motile Golgi bodies, which are connected to the ER by yet to be identified tethering factors. Previous studies indicated a role of cis-Golgi plant golgins (long coiled-coil domains proteins anchored to Golgi membranes) in Golgi biogenesis. Here we show a tethering role for the golgin AtCASP at the ER-Golgi interface. Using live-cell imaging, Golgi body dynamics were compared in Arabidopsis thaliana leaf epidermal cells expressing fluorescently tagged AtCASP, a truncated AtCASP-ΔCC lacking the coiled-coil domains, and the Golgi marker STtmd. Golgi body speed and displacement were significantly reduced in AtCASP-ΔCC lines. Using a dual-colour optical trapping system and a TIRF-tweezer system, individual Golgi bodies were captured in planta. Golgi bodies in AtCASP-ΔCC lines were easier to trap, and the ER-Golgi connection was more easily disrupted. Occasionally, the ER tubule followed a trapped Golgi body with a gap, indicating the presence of other tethering factors. Our work confirms that the intimate ER-Golgi association can be disrupted or weakened by expression of truncated AtCASP-ΔCC, and suggests that this connection is most likely maintained by a golgin-mediated tethering complex.

Highlight Here we show that the Golgi-associated Arabidopsis thaliana protein AtCASP may form part of a golgin-mediated tethering complex involved in anchoring plant Golgi stacks to the endoplasmic reticulum (ER).

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Posted March 14, 2017.
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Stacks off tracks: A role for the golgin AtCASP in plant endoplasmic reticulum – Golgi apparatus tethering
Anne Osterrieder, Stan W Botchway, Andy Ward, Tijs Ketelaar, Norbert de Ruijter, Chris Hawes
bioRxiv 115840; doi: https://doi.org/10.1101/115840
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Stacks off tracks: A role for the golgin AtCASP in plant endoplasmic reticulum – Golgi apparatus tethering
Anne Osterrieder, Stan W Botchway, Andy Ward, Tijs Ketelaar, Norbert de Ruijter, Chris Hawes
bioRxiv 115840; doi: https://doi.org/10.1101/115840

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