PMID- 10221984
OWN - NLM
STAT- MEDLINE
DCOM- 19990513
LR  - 20171213
IS  - 0031-9333 (Print)
IS  - 0031-9333 (Linking)
VI  - 79
IP  - 2
DP  - 1999 Apr
TI  - Vacuolar and plasma membrane proton-adenosinetriphosphatases.
PG  - 361-85
AB  - The vacuolar H+-ATPase (V-ATPase) is one of the most fundamental enzymes in
      nature. It functions in almost every eukaryotic cell and energizes a wide variety
      of organelles and membranes. V-ATPases have similar structure and mechanism of
      action with F-ATPase and several of their subunits evolved from common ancestors.
      In eukaryotic cells, F-ATPases are confined to the semi-autonomous organelles,
      chloroplasts, and mitochondria, which contain their own genes that encode some of
      the F-ATPase subunits. In contrast to F-ATPases, whose primary function in
      eukaryotic cells is to form ATP at the expense of the proton-motive force (pmf), 
      V-ATPases function exclusively as ATP-dependent proton pumps. The pmf generated
      by V-ATPases in organelles and membranes of eukaryotic cells is utilized as a
      driving force for numerous secondary transport processes. The mechanistic and
      structural relations between the two enzymes prompted us to suggest similar
      functional units in V-ATPase as was proposed to F-ATPase and to assign some of
      the V-ATPase subunit to one of four parts of a mechanochemical machine: a
      catalytic unit, a shaft, a hook, and a proton turbine. It was the yeast genetics 
      that allowed the identification of special properties of individual subunits and 
      the discovery of factors that are involved in the enzyme biogenesis and assembly.
      The V-ATPases play a major role as energizers of animal plasma membranes,
      especially apical plasma membranes of epithelial cells. This role was first
      recognized in plasma membranes of lepidopteran midgut and vertebrate kidney. The 
      list of animals with plasma membranes that are energized by V-ATPases now
      includes members of most, if not all, animal phyla. This includes the classical
      Na+ absorption by frog skin, male fertility through acidification of the sperm
      acrosome and the male reproductive tract, bone resorption by mammalian
      osteoclasts, and regulation of eye pressure. V-ATPase may function in Na+ uptake 
      by trout gills and energizes water secretion by contractile vacuoles in
      Dictyostelium. V-ATPase was first detected in organelles connected with the
      vacuolar system. It is the main if not the only primary energy source for
      numerous transport systems in these organelles. The driving force for the
      accumulation of neurotransmitters into synaptic vesicles is pmf generated by
      V-ATPase. The acidification of lysosomes, which are required for the proper
      function of most of their enzymes, is provided by V-ATPase. The enzyme is also
      vital for the proper function of endosomes and the Golgi apparatus. In contrast
      to yeast vacuoles that maintain an internal pH of approximately 5.5, it is
      believed that the vacuoles of lemon fruit may have a pH as low as 2. Similarly,
      some brown and red alga maintain internal pH as low as 0.1 in their vacuoles. One
      of the outstanding questions in the field is how such a conserved enzyme as the
      V-ATPase can fulfill such diverse functions.
FAU - Nelson, N
AU  - Nelson N
AD  - Department of Biochemistry, Faculty of Life Sciences, Tel Aviv University, Tel
      Aviv, Israel.
FAU - Harvey, W R
AU  - Harvey WR
LA  - eng
GR  - AI-22444/AI/NIAID NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, Non-P.H.S.
PT  - Research Support, U.S. Gov't, P.H.S.
PT  - Review
PL  - United States
TA  - Physiol Rev
JT  - Physiological reviews
JID - 0231714
RN  - 0 (Proton Pumps)
RN  - EC 3.6.1.- (Vacuolar Proton-Translocating ATPases)
RN  - EC 3.6.3.14 (Proton-Translocating ATPases)
SB  - IM
MH  - Animals
MH  - Cell Membrane/*enzymology
MH  - Epithelial Cells/enzymology
MH  - Male
MH  - Proton Pumps/*metabolism
MH  - Proton-Translocating ATPases/*metabolism
MH  - Spermatozoa/enzymology
MH  - *Vacuolar Proton-Translocating ATPases
MH  - Vacuoles/*enzymology
RF  - 233
EDAT- 1999/04/30 00:00
MHDA- 1999/04/30 00:01
CRDT- 1999/04/30 00:00
PHST- 1999/04/30 00:00 [pubmed]
PHST- 1999/04/30 00:01 [medline]
PHST- 1999/04/30 00:00 [entrez]
AID - 10.1152/physrev.1999.79.2.361 [doi]
PST - ppublish
SO  - Physiol Rev. 1999 Apr;79(2):361-85. doi: 10.1152/physrev.1999.79.2.361.