The main focus of our research is on the structure, function and regulation of V-ATPases. These universal proton pumps occur in every eukaryotic cell, mostly in membranes of acidic organelles, but also in animal plasma membranes. We are mainly interested in two aspects, the reversible dissociation of the V1VO holenzyme into its V1 and VO complexes, and the inhibitory influence of specific antibiotics.

   

Beschreibung: \\WSVTP\Wieczorek$\Daten\Aktuell\SFB 431\Abschluss-Reviews\2011 Review European Journal of Cell Biology\V-ATPase model-2a.tif

 

Selected publications

Meyer, H., Vitavska, O. and Wieczorek, H. (2011) Identification of the first animal sucrose transporter. J. Cell Science, in press

Bockelmann, S., Menche, D., Rudolph, S., Bender, T., Grond, S., von Zezschwitz, P., Stephen Muench, S., Wieczorek, H., and Huss, M. (2010) Archazolid A binds to the equatorial region of the c-ring of the vacuolar H+-ATPase. J. Biol. Chem. 285, 38304-38314

Muench, S.P., Huss, M., Phillips, C., Wieczorek, H., Trinick, J., and Harrison, M.A. (2009) Cryo-electron microscopy of the vacuolar ATPase motor reveals its mechanical and regulatory complexity. J. Mol. Biol. 386, 989-999

Vitavska, O., Merzendorfer, H., and Wieczorek, H. (2005) The V-ATPase subunit C binds to polymeric F-actin as well as to monomeric G-actin and induces cross-linking of actin filaments. J. Biol. Chem. 280, 1070-1076

Sumner, J.P., Dow, J.A.T., Earley, F., Klein, U., Jäger, D., and Wieczorek, H. (1995) Regulation of plasma membrane V-ATPase activity by dissociation of peripheral subunits. J. Biol. Chem. 270, 5649-5653