caa a22 4500 463208439 CHVBK 20180405153133.0 cr unu---uuuuu 170326e20071201xx s 000 0 eng 10.1007/s10863-007-9112-z doi (NATIONALLICENCE)springer-10.1007/s10863-007-9112-z Kane Patricia Department of Biochemistry and Molecular Biology, SUNY Upstate Medical University, 13210, Syracuse, NY, USA aut The long physiological reach of the yeast vacuolar H+-ATPase [Elektronische Daten] [Patricia Kane] V-ATPases are structurally conserved and functionally versatile proton pumps found in all eukaryotes. The yeast V-ATPase has emerged as a major model system, in part because yeast mutants lacking V-ATPase subunits (vma mutants) are viable and exhibit a distinctive Vma- phenotype. Yeast vma mutants are present in ordered collections of all non-essential yeast deletion mutants, and a number of additional phenotypes of these mutants have emerged in recent years from genomic screens. This review summarizes the many phenotypes that have been associated with vma mutants through genomic screening. The results suggest that V-ATPase activity is important for an unexpectedly wide range of cellular processes. For example, vma mutants are hypersensitive to multiple forms of oxidative stress, suggesting an antioxidant role for the V-ATPase. Consistent with such a role, vma mutants display oxidative protein damage and elevated levels of reactive oxygen species, even in the absence of an exogenous oxidant. This endogenous oxidative stress does not originate at the electron transport chain, and may be extra-mitochondrial, perhaps linked to defective metal ion homeostasis in the absence of a functional V-ATPase. Taken together, genomic data indicate that the physiological reach of the V-ATPase is much longer than anticipated. Further biochemical and genetic dissection is necessary to distinguish those physiological effects arising directly from the enzyme's core functions in proton pumping and organelle acidification from those that reflect broader requirements for cellular pH homeostasis or alternative functions of V-ATPase subunits. Springer Science+Business Media, LLC, 2007 V-ATPase nationallicence Yeast nationallicence vma mutant nationallicence Acidification nationallicence Genomic nationallicence Oxidative stress nationallicence Journal of Bioenergetics and Biomembranes Springer US; http://www.springer-ny.com 39/5-6(2007-12-01), 415-421 0145-479X 39:5-6<415 2007 39 10863 https://doi.org/10.1007/s10863-007-9112-z text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/s10863-007-9112-z text/html Onlinezugriff via DOI NATIONALLICENCE 100 1- Kane Patricia Department of Biochemistry and Molecular Biology, SUNY Upstate Medical University, 13210, Syracuse, NY, USA aut NATIONALLICENCE 773 0- Journal of Bioenergetics and Biomembranes Springer US; http://www.springer-ny.com 39/5-6(2007-12-01), 415-421 0145-479X 39:5-6<415 2007 39 10863 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer