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The odd one out:Arabidopsisreticulon20 has a role in lipid biosynthesis

Authors :
Jessica Upson
Patrick Moreau
Louise Hughes
Maike Kittelmann
Chris Hawes
Stanley W. Botchway
Jake Richardson
Verena Kriechbaumer
Lilly Maneta-Peyret
Publication Year :
2017
Publisher :
Cold Spring Harbor Laboratory, 2017.

Abstract

The family of reticulon proteins has been shown to be involved in a variety of functions in eukaryotic cells including tubulation of the endoplasmic reticulum (ER), formation of cell plates and primary plasmodesmata. Reticulons are integral ER membrane proteins characterised by a reticulon homology domain comprising four transmembrane domains which results in the reticulons sitting in the membrane in a W-topology. Here we report on a subgroup of reticulons with an extended N-terminal domain and in particular on arabidopsis reticulon 20. We show that reticulon 20 is located in a unique punctate pattern on the ER membrane. Its closest homologue reticulon 19 labels the whole ER. We show that mutants in RTN20 or RTN19, respectively, display a significant change in sterol composition in the roots indicating a role in lipid biosynthesis or regulation. A third homologue in this family - 3BETAHSD/D1- is localised to ER exit sites resulting in an intriguing location difference for the three proteins.

Details

Database :
OpenAIRE
Accession number :
edsair.doi.dedup.....e612fe553c009da2dd64232b17a83762
Full Text :
https://doi.org/10.1101/123679