@article {Kriechbaumer123679, author = {Verena Kriechbaumer and Lilly Maneta-Peyret and Stanley W Botchway and Jessica Upson and Louise Hughes and Jake Richardson and Maike Kittelmann and Patrick Moreau and Chris Hawes}, title = {The odd one out: Arabidopsis reticulon20 has a role in lipid biosynthesis}, elocation-id = {123679}, year = {2017}, doi = {10.1101/123679}, publisher = {Cold Spring Harbor Laboratory}, 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.}, URL = {https://www.biorxiv.org/content/early/2017/04/07/123679}, eprint = {https://www.biorxiv.org/content/early/2017/04/07/123679.full.pdf}, journal = {bioRxiv} }