Vacuolar proton-translocating inorganic pyrophosphatases (VPPases) are proton transporters activating vacuolar secondary transport systems by establishing proton gradient across the endomembrane. V-PPase, a simple proton pump with 13-16 transmembrane helices compactly folded in a rosette manner in two concentric walls. VPPases have three highly conserved motifs CS1, CS2 and CS3 which regulates the translocation of H+ ions from cytosol to vacuolar lumen. The pumping of H+ into vacuole builds electrochemical gradient which changes its pH and energizes various antiporters resulting in influx of Na+ , K+ , NO3 - , Cl- from cytosol to vacuole and reduces the toxicity in cytosol. This review presents an overview on 3-D structure, motifs, function and working model of VPPases under salt stress.
