Reference: Singh MK, et al. (2014) Protein delivery to vacuole requires SAND protein-dependent Rab GTPase conversion for MVB-vacuole fusion. Curr Biol 24(12):1383-1389

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Abstract


Plasma-membrane proteins such as ligand-binding receptor kinases, ion channels, or nutrient transporters are turned over by targeting to a lytic compartment--lysosome or vacuole--for degradation. After their internalization, these proteins arrive at an early endosome, which then matures into a late endosome with intraluminal vesicles (multivesicular body, MVB) before fusing with the lysosome/vacuole in animals or yeast. The endosomal maturation step involves a SAND family protein mediating Rab5-to-Rab7 GTPase conversion. Vacuolar trafficking is much less well understood in plants. Here we analyze the role of the single-copy SAND gene of Arabidopsis. In contrast to its animal or yeast counterpart, Arabidopsis SAND protein is not required for early-to-late endosomal maturation, although its role in mediating Rab5-to-Rab7 conversion is conserved. Instead, Arabidopsis SAND protein is essential for the subsequent fusion of MVBs with the vacuole. The inability of sand mutant to mediate MVB-vacuole fusion is not caused by the continued Rab5 activity but rather reflects the failure to activate Rab7. In conclusion, regarding the endosomal passage of cargo proteins for degradation, a major difference between plants and nonplant organisms might result from the relative timing of endosomal maturation and SAND-dependent Rab GTPase conversion as a prerequisite for the fusion of late endosomes/MVBs with the lysosome/vacuole.

Reference Type
Journal Article | Research Support, Non-U.S. Gov't
Authors
Singh MK, Krüger F, Beckmann H, Brumm S, Vermeer JEM, Munnik T, Mayer U, Stierhof YD, Grefen C, Schumacher K, ... Show all
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