Plant RMR proteins: unique vacuolar sorting receptors that couple ligand sorting with membrane internalization

被引:27
|
作者
Wang, Hao [1 ,3 ]
Rogers, John C. [2 ]
Jiang, Liwen [1 ,3 ]
机构
[1] Chinese Univ Hong Kong, State China Key Lab Agrobaiotechnol, Shatin, Hong Kong, Peoples R China
[2] Washington State Univ, Inst Biol Chem, Pullman, WA 99164 USA
[3] Chinese Univ Hong Kong, Dept Biol, Ctr Cell & Dev Biol, Shatin, Hong Kong, Peoples R China
关键词
lytic PVC; PA domain; pollen tube; PSV; receptor; RING-H2; domain; RMR; storage PVC; vacuole; VSR; E3 UBIQUITIN LIGASE; STORAGE PROTEINS; PREVACUOLAR COMPARTMENTS; MULTIVESICULAR BODIES; GOLGI-APPARATUS; CELLS; ARABIDOPSIS; DOMAIN; BP-80; IDENTIFICATION;
D O I
10.1111/j.1742-4658.2010.07923.x
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
收藏
页码:59 / 68
页数:10
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