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Published online 22 August 2005. doi:10.1083/jcb.200504112
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 170, Number 5, 757-767
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Article

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



Misoon Park, Daeseok Lee, Gil-Je Lee, and Inhwan Hwang

Division of Molecular and Life Sciences, Center for Plant Intracellular Trafficking, Pohang University of Science and Technology, Pohang 790-784, Korea

Correspondence to Inhwan Hwang: ihhwang{at}postech.ac.kr

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 (AtRMR) 1 plays in protein trafficking to the PSV. AtRMR1 mainly colocalized to the prevacuolar compartment of the PSV, but a minor portion also localized to the Golgi complex. The coexpression of AtRMR1 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. Coimmunoprecipitation and in vitro binding assays revealed that the lumenal domain of AtRMR1 interacts with the COOH-terminal sorting signal of phaseolin at acidic pH. Furthermore, phaseolin colocalized with AtRMR1 on its way to the PSV. Based on these results, we propose that AtRMR1 functions as the sorting receptor of phaseolin for its trafficking to the PSV.

Abbreviations used in this paper: AALP, Arabidopsis aleurain-like protease; AtRMR, Arabidopsis thaliana RMR; BiP, binding protein; COP, coat protein complex; CT, cytosolic tail; CTPP, COOH-terminal propeptide; DIP, dark-induced tonoplastic intrinsic protein; DV, dense vesicle; LU, lumenal domain; MBP, maltose-binding protein; NTPP, NH2-terminal propeptide; PAC, precursor accumulating; PSV, protein storage vacuole; PVC, prevacuolar compartment; RMR, receptor homology region transmembrane domain ring H2 motif protein; ST, sialyltransferase; TIP, tonoplast intrinsic protein; VSR, vacuolar sorting receptor.


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