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Open Access Research article

Ubiquitin initiates sorting of Golgi and plasma membrane proteins into the vacuolar degradation pathway

David Scheuring2, Fabian Künzl1, Corrado Viotti23, Melody San Wan Yan4, Liwen Jiang4, Swen Schellmann5, David G Robinson2 and Peter Pimpl12*

Author Affiliations

1 Department of Developmental Genetics, Center for Plant Molecular Biology (ZMBP), University of Tübingen, Tübingen, 72076, Germany

2 Department of Plant Cell Biology, Centre for Organismal Studies, University of Heidelberg, Heidelberg, 69120, Germany

3 Plant Developmental Biology, Centre for Organismal Studies, University of Heidelberg, Heidelberg, 69120, Germany

4 School of Life Sciences, Centre for Cell and Developmental Biology, The Chinese University of Hong Kong, Shatin NT, Hong Kong, PR China

5 Botanical Institute, Biozentrum Köln, University of Cologne, Cologne, 50674, Germany

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BMC Plant Biology 2012, 12:164  doi:10.1186/1471-2229-12-164

Published: 12 September 2012

Abstract

Background

In yeast and mammals, many plasma membrane (PM) proteins destined for degradation are tagged with ubiquitin. These ubiquitinated proteins are internalized into clathrin-coated vesicles and are transported to early endosomal compartments. There, ubiquitinated proteins are sorted by the endosomal sorting complex required for transport (ESCRT) machinery into the intraluminal vesicles of multivesicular endosomes. Degradation of these proteins occurs after endosomes fuse with lysosomes/lytic vacuoles to release their content into the lumen. In plants, some PM proteins, which cycle between the PM and endosomal compartments, have been found to be ubiquitinated, but it is unclear whether ubiquitin is sufficient to mediate internalization and thus acts as a primary sorting signal for the endocytic pathway. To test whether plants use ubiquitin as a signal for the degradation of membrane proteins, we have translationally fused ubiquitin to different fluorescent reporters for the plasma membrane and analyzed their transport.

Results

Ubiquitin-tagged PM reporters localized to endosomes and to the lumen of the lytic vacuole in tobacco mesophyll protoplasts and in tobacco epidermal cells. The internalization of these reporters was significantly reduced if clathrin-mediated endocytosis was inhibited by the coexpression of a mutant of the clathrin heavy chain, the clathrin hub. Surprisingly, a ubiquitin-tagged reporter for the Golgi was also transported into the lumen of the vacuole. Vacuolar delivery of the reporters was abolished upon inhibition of the ESCRT machinery, indicating that the vacuolar delivery of these reporters occurs via the endocytic transport route.

Conclusions

Ubiquitin acts as a sorting signal at different compartments in the endomembrane system to target membrane proteins into the vacuolar degradation pathway: If displayed at the PM, ubiquitin triggers internalization of PM reporters into the endocytic transport route, but it also mediates vacuolar delivery if displayed at the Golgi. In both cases, ubiquitin-tagged proteins travel via early endosomes and multivesicular bodies to the lytic vacuole. This suggests that vacuolar degradation of ubiquitinated proteins is not restricted to PM proteins but might also facilitate the turnover of membrane proteins in the early secretory pathway.