AtRMR1 functions as a cargo receptor for protein trafficking to the protein storage vacuole.

Organellar proteins are sorted by cargo receptors on the way to their final destination. However, receptors for proteins that are destined for the protein storage vacuole (PSV) are largely unknown. In this study, we investigated the biological role that Arabidopsis thaliana receptor homology region transmembrane domain ring H2 motif protein 1 plays in protein trafficking to the PSV. mainly colocalized to the prevacuolar compartment of the PSV, but a minor portion also localized to the Golgi complex. The coexpression of Atduanyu17481 mutants that were localized to the Golgi complex strongly inhibited the trafficking of phaseolin to the PSV and caused accumulation of phaseolin in the Golgi complex or its secretion. Co-immunoprecipitation and in vitro binding assays revealed that the lumenal domain of Atduanyu17481 interacts with the COOH-terminal sorting signal of phaseolin at acidic pH. Furthermore, phaseolin colocalized with Atduanyu17481 on its way to the PSV. Based on these results, we propose that Atduanyu17481 functions as the sorting receptor of phaseolin for its trafficking to the PSV.

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