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RMR (Receptor Membrane RING-H2) type 1 and 2 show different promoter activities and subcellular localizations in Arabidopsis thaliana.
Journal article

RMR (Receptor Membrane RING-H2) type 1 and 2 show different promoter activities and subcellular localizations in Arabidopsis thaliana.

  • Occhialini A Department of Food Science, University of Tennessee, Food Safety and Processing Building, 2600 River Dr., Knoxville, TN 37996, USA; Institute of Biology, Laboratory of Cell and Molecular Biology, University of Neuchâtel, Rue Emile-Argand 11, CH-2000 Neuchâtel, Switzerland. Electronic address: aocchial@utk.edu.
  • Marc-Martin S Institute of Biology, Laboratory of Cell and Molecular Biology, University of Neuchâtel, Rue Emile-Argand 11, CH-2000 Neuchâtel, Switzerland.
  • Gouzerh G Institute of Biology, Laboratory of Cell and Molecular Biology, University of Neuchâtel, Rue Emile-Argand 11, CH-2000 Neuchâtel, Switzerland.
  • Hillmer S Electron Microscopy Core Facility, University of Heidelberg, Im Neuenheimer Feld 345, 69120 Heidelberg, Germany.
  • Neuhaus JM Institute of Biology, Laboratory of Cell and Molecular Biology, University of Neuchâtel, Rue Emile-Argand 11, CH-2000 Neuchâtel, Switzerland. Electronic address: jean-marc.neuhaus@unine.ch.
  • 2017-12-16
Published in:
  • Plant science : an international journal of experimental plant biology. - 2018
Arabidopsis thaliana
AtRMR endogenous promoters
AtRMRs
Endoplasmic reticulum
Transmission electron microscopy
trans-Golgi network
Arabidopsis
Arabidopsis Proteins
Membrane Proteins
Organ Specificity
Plant Cells
Plant Leaves
Plants, Genetically Modified
Protoplasts
English Soluble vacuolar proteins reach their compartments of final accumulation through the binding with specific transmembrane cargo receptors. In Arabidopsis thaliana two different families of receptors have been characterized. The AtVSRs (Vacuolar Sorting Receptor), which are known to be involved in the protein sorting to lytic vacuoles (LV), and the AtRMRs (Receptor Membrane RING-H2), for which there is less evidence for a role in the traffic to the protein storage vacuole (PSV). In this study we investigated the localization and tissue expression of two RMRs (AtRMR1 and 2) in their species of origin, A. thaliana. Our experiments using leaf protoplasts and transgenic plants supported previous results of subcellular localization in Nicotiana benthamiana that visualized AtRMR1 and 2 in the cisternae of endoplasmic reticulum (ER) and in the trans-Golgi network (TGN), respectively. The promoter activities of AtRMR1 and AtRMR2 detected in transgenic A. thaliana lines suggest that the expression of these two receptors only partially overlap in some organs and tissues. These results suggest that AtRMR1 and 2 are not functionally redundant, but could also interact and participate in the same cellular process in tissues with an overlapping expression.
Language
  • English
Open access status
closed
Identifiers
Persistent URL
https://sonar.ch/global/documents/186510
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