The odd one out: Arabidopsis reticulon 20 does not bend ER membranes but has a role in lipid regulation

Reticulons are integral ER membrane proteins characterised by a reticulon homology domain comprising four transmembrane domains which results in the proteins sitting in the membrane in a W-topology. Here we report on a novel subgroup of reticulons with an extended N-terminal domain and in particular...

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Bibliographic Details
Published in:Scientific reports 2018-02, Vol.8 (1), p.2310-15, Article 2310
Main Authors: Kriechbaumer, Verena, Maneta-Peyret, Lilly, Fouillen, Laetitia, Botchway, Stanley W., Upson, Jessica, Hughes, Louise, Richardson, Jake, Kittelmann, Maike, Moreau, Patrick, Hawes, Chris
Format: Article
Language:English
Subjects:
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Arabidopsis - metabolism
Arabidopsis Proteins - metabolism
Confocal microscopy
Endoplasmic Reticulum - metabolism
Homology
Humanities and Social Sciences
Life Sciences
Lipid Metabolism
Membrane proteins
Membrane Proteins - metabolism
Membranes
Microscopy, Confocal
Microscopy, Fluorescence
multidisciplinary
Proteins
Science
Science (multidisciplinary)
Sterol composition
Topology
Transmembrane domains
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Summary:Reticulons are integral ER membrane proteins characterised by a reticulon homology domain comprising four transmembrane domains which results in the proteins sitting in the membrane in a W-topology. Here we report on a novel subgroup of reticulons with an extended N-terminal domain and in particular on arabidopsis reticulon 20. Using high resolution confocal microscopy 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. Other than demonstrated for the other members of the reticulon protein family RTN20 and 19 do not display ER constriction phenotypes on over expression. We show that mutants in RTN20 or RTN19, respectively, display a significant change in sterol composition in roots indicating a role in lipid regulation. A third homologue in this family -3BETAHSD/D1- is unexpectedly localised to ER exit sites resulting in an intriguing location difference for the three proteins.
ISSN:2045-2322
2045-2322
DOI:10.1038/s41598-018-20840-0