caa a22 4500 463208307 CHVBK 20180405153132.0 cr unu---uuuuu 170326e20071201xx s 000 0 eng 10.1007/s10863-007-9116-8 doi (NATIONALLICENCE)springer-10.1007/s10863-007-9116-8 The vacuolar (H+)-ATPase: subunit arrangement and in vivo regulation [Elektronische Daten] [Jie Qi, Yanru Wang, Michael Forgac] The V-ATPases are responsible for acidification of intracellular compartments and proton transport across the plasma membrane. They play an important role in both normal processes, such as membrane traffic, protein degradation, urinary acidification, and bone resorption, as well as various disease processes, such as viral infection, toxin killing, osteoporosis, and tumor metastasis. V-ATPases contain a peripheral domain (V1) that carries out ATP hydrolysis and an integral domain (V0) responsible for proton transport. V-ATPases operate by a rotary mechanism involving both a central rotary stalk and a peripheral stalk that serves as a stator. Cysteine-mediated cross-linking has been used to localize subunits within the V-ATPase complex and to investigate the helical interactions between subunits within the integral V0 domain. An essential property of the V-ATPases is the ability to regulate their activity in vivo. An important mechanism of regulating V-ATPase activity is reversible dissociation of the complex into its component V1 and V0 domains. The dependence of reversible dissociation on subunit isoforms and cellular environment has been investigated. Springer Science+Business Media, LLC, 2007 ATPase nationallicence V1 and V0 domains nationallicence Subunit isoforms nationallicence Qi Jie Department of Physiology, Tufts University School of Medicine, 136 Harrison Ave., 02111, Boston, MA, USA aut Wang Yanru Department of Physiology, Tufts University School of Medicine, 136 Harrison Ave., 02111, Boston, MA, USA aut Forgac Michael Department of Physiology, Tufts University School of Medicine, 136 Harrison Ave., 02111, Boston, MA, USA aut Journal of Bioenergetics and Biomembranes Springer US; http://www.springer-ny.com 39/5-6(2007-12-01), 423-426 0145-479X 39:5-6<423 2007 39 10863 https://doi.org/10.1007/s10863-007-9116-8 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/s10863-007-9116-8 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Qi Jie Department of Physiology, Tufts University School of Medicine, 136 Harrison Ave., 02111, Boston, MA, USA aut NATIONALLICENCE 700 1- Wang Yanru Department of Physiology, Tufts University School of Medicine, 136 Harrison Ave., 02111, Boston, MA, USA aut NATIONALLICENCE 700 1- Forgac Michael Department of Physiology, Tufts University School of Medicine, 136 Harrison Ave., 02111, Boston, MA, USA aut NATIONALLICENCE 773 0- Journal of Bioenergetics and Biomembranes Springer US; http://www.springer-ny.com 39/5-6(2007-12-01), 423-426 0145-479X 39:5-6<423 2007 39 10863 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer