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Open AccessArticle

Dimerization of the Vacuolar Receptors AtRMR1 and -2 from Arabidopsis thaliana Contributes to Their Localization in the trans-Golgi Network

1
Plant Biology and Crop Science, Rothamsted Research, Harpenden, AL5 2JQ Herts, UK
2
Laboratory of Cell and Molecular Biology, Institute of Biology, University of Neuchâtel, Rue Emile-Argand 11, CH-2009 Neuchâtel, Switzerland
3
DISTEBA, Department of Biological and Environmental Sciences and Technologies, University of Salento, Campus Ecotekne, 73100 Lecce, Italy
*
Authors to whom correspondence should be addressed.
Academic Editor: Gregor Drummen
Int. J. Mol. Sci. 2016, 17(10), 1661; https://doi.org/10.3390/ijms17101661
Received: 22 July 2016 / Revised: 23 September 2016 / Accepted: 23 September 2016 / Published: 30 September 2016
(This article belongs to the Special Issue Unconventional Proteins and Membranes Traffic)
In Arabidopsis thaliana, different types of vacuolar receptors were discovered. The AtVSR (Vacuolar Sorting Receptor) receptors are well known to be involved in the traffic to lytic vacuole (LV), while few evidences demonstrate the involvement of the receptors from AtRMR family (Receptor Membrane RING-H2) in the traffic to the protein storage vacuole (PSV). In this study we focused on the localization of two members of AtRMR family, AtRMR1 and -2, and on the possible interaction between these two receptors in the plant secretory pathway. Our experiments with agroinfiltrated Nicotiana benthamiana leaves demonstrated that AtRMR1 was localized in the endoplasmic reticulum (ER), while AtRMR2 was targeted to the trans-Golgi network (TGN) due to the presence of a cytosolic 23-amino acid sequence linker. The fusion of this linker to an equivalent position in AtRMR1 targeted this receptor to the TGN, instead of the ER. By using a Bimolecular Fluorescent Complementation (BiFC) technique and experiments of co-localization, we demonstrated that AtRMR2 can make homodimers, and can also interact with AtRMR1 forming heterodimers that locate to the TGN. Such interaction studies strongly suggest that the transmembrane domain and the few amino acids surrounding it, including the sequence linker, are essential for dimerization. These results suggest a new model of AtRMR trafficking and dimerization in the plant secretory pathway. View Full-Text
Keywords: AtRMR; PA domain; RING-H2; Ser-Rich domain; linker; transmembrane; plant secretory pathway; trans-Golgi network; endoplasmic reticulum; dimerization; laser scanning confocal microscopy; Bimolecular Fluorescent Complementation; Arabidopsis thaliana; Nicotiana benthamiana AtRMR; PA domain; RING-H2; Ser-Rich domain; linker; transmembrane; plant secretory pathway; trans-Golgi network; endoplasmic reticulum; dimerization; laser scanning confocal microscopy; Bimolecular Fluorescent Complementation; Arabidopsis thaliana; Nicotiana benthamiana
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MDPI and ACS Style

Occhialini, A.; Gouzerh, G.; Di Sansebastiano, G.-P.; Neuhaus, J.-M. Dimerization of the Vacuolar Receptors AtRMR1 and -2 from Arabidopsis thaliana Contributes to Their Localization in the trans-Golgi Network. Int. J. Mol. Sci. 2016, 17, 1661. https://doi.org/10.3390/ijms17101661

AMA Style

Occhialini A, Gouzerh G, Di Sansebastiano G-P, Neuhaus J-M. Dimerization of the Vacuolar Receptors AtRMR1 and -2 from Arabidopsis thaliana Contributes to Their Localization in the trans-Golgi Network. International Journal of Molecular Sciences. 2016; 17(10):1661. https://doi.org/10.3390/ijms17101661

Chicago/Turabian Style

Occhialini, Alessandro; Gouzerh, Guillaume; Di Sansebastiano, Gian-Pietro; Neuhaus, Jean-Marc. 2016. "Dimerization of the Vacuolar Receptors AtRMR1 and -2 from Arabidopsis thaliana Contributes to Their Localization in the trans-Golgi Network" Int. J. Mol. Sci. 17, no. 10: 1661. https://doi.org/10.3390/ijms17101661

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