@misc{BaumannWalz2012,
  author    = {Baumann, Otto and Walz, Bernd},
  title     = {The blowfly salivary gland - A model system for analyzing the regulation of plasma membrane V-ATPase},
  series = {Journal of insect physiology},
  volume    = {58},
  journal   = {Journal of insect physiology},
  number    = {4},
  publisher = {Elsevier},
  address   = {Oxford},
  issn      = {0022-1910},
  doi       = {10.1016/j.jinsphys.2011.11.015},
  pages     = {450 -- 458},
  year      = {2012},
  abstract  = {Vacuolar H+-ATPases (V-ATPases) are heteromultimeric proteins that use the energy of ATP hydrolysis for the electrogenic transport of protons across membranes. They are common to all eukaryotic cells and are located in the plasma membrane or in membranes of acid organelles. In many insect epithelia, V-ATPase molecules reside in large numbers in the apical plasma membrane and create an electrochemical proton gradient that is used for the acidification or alkalinization of the extracellular space, the secretion or reabsorption of ions and fluids, the import of nutrients, and diverse other cellular activities. Here, we summarize our results on the functions and regulation of V-ATPase in the tubular salivary gland of the blowfly Calliphora vicina. In this gland, V-ATPase activity energizes the secretion of a KCl-rich saliva in response to the neurohormone serotonin (5-HT). Because of particular morphological and physiological features, the blowfly salivary glands are a superior and exemplary system for the analysis of the intracellular signaling pathways and mechanisms that modulate V-ATPase activity and solute transport in an insect epithelium.},
  language  = {en}
}
@article{BaumannWalz2001,
  author    = {Baumann, Otto and Walz, Bernd},
  title     = {The endoplasmic reticulum of animal cells and its organization into structural and functional domains},
  year      = {2001},
  language  = {en}
}
@misc{VossBlenauWalzetal.2009,
  author    = {Voss, Martin and Blenau, Wolfgang and Walz, Bernd and Baumann, Otto},
  title     = {V-ATPase deactivation in blowfly salivary glands is mediated by protein phosphatase 2C},
  url       = {http://nbn-resolving.de/urn:nbn:de:kobv:517-opus-44360},
  year      = {2009},
  abstract  = {The activity of vacuolar H+-ATPase (V-ATPase) in the apical membrane of blowfly (Calliphora vicina) salivary glands is regulated by the neurohormone serotonin (5-HT). 5-HT induces, via protein kinase A, the phosphorylation of V-ATPase subunit C and the assembly of V-ATPase holoenzymes. The protein phosphatase responsible for the dephosphorylation of subunit C and V-ATPase inactivation is not as yet known. We show here that inhibitors of protein phosphatases PP1 and PP2A (tautomycin, ocadaic acid) and PP2B (cyclosporin A, FK-506) do not prevent V-ATPase deactivation and dephosphorylation of subunit C. A decrease in the intracellular Mg2+ level caused by loading secretory cells with EDTA-AM leads to the activation of proton pumping in the absence of 5-HT, prolongs the 5-HT-induced response in proton pumping, and inhibits the dephosphorylation of subunit C. Thus, the deactivation of V-ATPase is most probably mediated by a protein phosphatase that is insensitive to okadaic acid and that requires Mg2+, namely, a member of the PP2C protein family. By molecular biological techniques, we demonstrate the expression of at least two PP2C protein family members in blowfly salivary glands. © 2009 Wiley Periodicals, Inc.},
  language  = {en}
}