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

© The Author 2017. Published by Oxford University Press on behalf of the Society for Experimental Biology.

Bibliographische Detailangaben
Veröffentlicht in:Journal of experimental botany. - 1985. - 68(2017), 13 vom: 15. Juni, Seite 3339-3350
1. Verfasser: Osterrieder, Anne (VerfasserIn)
Weitere Verfasser: Sparkes, Imogen A, Botchway, Stan W, Ward, Andy, Ketelaar, Tijs, de Ruijter, Norbert, Hawes, Chris
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2017
Zugriff auf das übergeordnete Werk:Journal of experimental botany
Schlagworte:Journal Article Arabidopsis Golgi apparatus endomembrane system endoplasmic reticulum golgin optical tweezers secretory pathway tethering factor Arabidopsis Proteins mehr... CASP protein, Arabidopsis Golgi Matrix Proteins Membrane Proteins
Beschreibung
Zusammenfassung:© The Author 2017. Published by Oxford University Press on behalf of the Society for Experimental Biology.
The plant Golgi apparatus modifies and sorts incoming proteins from the endoplasmic reticulum (ER) and synthesizes 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 for cis-Golgi plant golgins, which are long coiled-coil domain 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
Beschreibung:Date Completed 22.02.2018
Date Revised 08.11.2024
published: Print
CommentIn: J Exp Bot. 2017 Jun 15;68(13):3283-3285. doi: 10.1093/jxb/erx216. - PMID 28859381
Citation Status MEDLINE
ISSN:1460-2431
DOI:10.1093/jxb/erx167