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Plant RMR proteins: unique vacuolar sorting receptors that couple ligand sorting with membrane internalization
Author(s) -
Wang Hao,
Rogers John C.,
Jiang Liwen
Publication year - 2011
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/j.1742-4658.2010.07923.x
Subject(s) - internalization , microbiology and biotechnology , vacuole , protein targeting , vacuolar protein sorting , biology , receptor , endomembrane system , transmembrane protein , biochemistry , membrane protein , endoplasmic reticulum , membrane , golgi apparatus , cytoplasm
In receptor‐mediated sorting of soluble protein ligands in the endomembrane system of eukaryotic cells, three completely different receptor proteins for mammalian (mannose 6‐phosphate receptor), yeast (Vps10p) and plant cells (vacuolar sorting receptor; VSR) have in common the features of pH‐dependent ligand binding and receptor recycling. In striking contrast, the plant receptor homology‐transmembrane‐RING‐H2 (RMR) proteins serve as sorting receptors to a separate type of vacuole, the protein storage vacuole, but do not recycle, and their trafficking pathway results in their internalization into the destination vacuole. Even though plant RMR proteins share high sequence similarity with the best‐characterized mammalian PA‐TM‐RING family proteins, these two families of proteins appear to play distinctly different roles in plant and animal cells. Thus, this minireview focuses on this unique sorting mechanism and traffic of RMR proteins via dense vesicles in various plant cell types.