In the latest issue of Science, Professor John Rubinstein‘s lab reports the first high-resolution structure of a mammalian V-ATPase. These ATP-hydrolysis–driven proton pumps are essential for acidification of endosomes, lysosomes, and the trans Golgi network, as well as for acid secretion by osteoclasts, kidney intercalated cells, and some tumor cells.
ATP hydrolysis in the V-ATPase catalytic V1 region drives rotation of a central rotor subcomplex and leads to proton translocation through the membrane-embedded VO region. For more see the Rubinstein’s Lab tweet.