Dimerization of the vacuolar receptors AtRMR1 and-2 from Arabidopsis thaliana contributes to their localization in the trans-Golgi Network

A - Papers appearing in refereed journals

Occhialini, A., Gouzerh, G., Di Sansebastiano, G. P. and Neuhaus, J. M. 2016. 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. 17 (10), p. 1661. https://doi.org/10.3390/ijms17101661

AuthorsOcchialini, A., Gouzerh, G., Di Sansebastiano, G. P. and Neuhaus, J. M.
Abstract

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.

KeywordsAtRMR; 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
Year of Publication2016
JournalInternational Journal Of Molecular Sciences
Journal citation17 (10), p. 1661
Digital Object Identifier (DOI)https://doi.org/10.3390/ijms17101661
PubMed ID27706038
PubMed Central IDPMC5085694
Open accessPublished as ‘gold’ (paid) open access
FunderBiotechnology and Biological Sciences Research Council
Funder project or codeWheat
[20:20 Wheat] Maximising yield potential of wheat
Publisher's version
Output statusPublished
Publication dates
Online30 Sep 2016
Publication process dates
Accepted23 Sep 2016
PublisherMDPI
MDPI
Copyright licenseCC BY
ISSN1422-0067

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