The V-type H+ ATPase: molecular structure and function,physiological roles and regulation

Beyenbach, Klaus W.; Wieczorek, Helmut

doi:10.1242/jeb.02014

Cited by 562 publications

(490 citation statements)

References 145 publications

(99 reference statements)

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“…Taking the ratios of the mean concentrations one concludes that in 10 min 17149.5 Pi molecules, i.e., 28.58 per second, were liberated by each V-ATPase molecules. Current understanding of the V-ATPase catalysis assume a hydrolysis of 3 ATP molecules in a complete 360 degrees rotation cycle (see., e.g., (Beyenbach and Wieczorek 2006)), which means that the rotation rate in V-ATPase in our vacuolar membrane vesicle system is 9.53 Hz at 20 °C and under excess ATP condition. If we consider the ± standard deviation of the fitting parameter P t , i.e., the one with the largest relative fitting error, the range of rotation rates is 6.2 − 21.1 Hz.…”

Section: Atpase Activity Assaymentioning

confidence: 93%

“…Similarly to the more familiar and related F-ATP synthase (FATPase) there are 3 catalytic sites, here for ATP hydrolysis, in the water soluble V 1 domain (F 1 domain in F-ATPase), and trans-membrane proton transport takes places in hydrophilic channels (or sacks) in the interface between the "c ring" and subunit a of the membrane bound V o (F o ) domain (Wilkens et al 1999;Grabe et al 2000;KawasakiNishi et al 2001;Wang et al 2004;Beyenbach and Wieczorek 2006) (Fig. 1).…”

Section: Introductionmentioning

confidence: 99%

“…In the case of V-ATPase rotation is driven by ATP binding and hydrolysis. One ATP molecule drives a 120 degrees rotation of the rotor and a transport of two protons from the cytoplasmic side to the "other" side, which can be the lumen of intracellular organs or the extracellular space, depending on the cellular location of V-ATPase (Finbow and Harrison 1997;Nishi and Forgac 2002;Beyenbach and Wieczorek 2006;Cipriano et al 2008;Jefferies et al 2008). This stoichiomerty is different form that of F-ATPase, in which there are ~12 c subunits, which have only 2 trans-membrane helices, each with a unique glutamic acid.…”

Section: Introductionmentioning

confidence: 99%

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Estimating the rotation rate in the vacuolar proton-ATPase in native yeast vacuolar membranes

et al. 2012

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The rate of rotation of the rotor of the yeast vacuolar proton-ATPase (V-ATPase), relative to the stator or the steady parts of enzyme, is estimated in native vacuolar membrane vesicles of Saccharomyces cerevisiae under standardised conditions. Membrane vesicles are spontaneously formed after exposing purified yeast vacuoles to osmotic shock. The fraction of the total ATPase activity originating from V-ATPase is determined using the potent and specific inhibitor of the enzyme, concanamycin A. Inorganic phosphate liberated from ATP in the vacuolar membrane vesicle system, during 10 min of ATPase activity at 20 °C, is assayed spectrophotometrically for different concanamycin A concentrations. A fit to the quadratic binding equation, assuming a single concanamycin A binding site on a monomeric V-ATPase (our data is incompatible with models assuming more binding sites) to the inhibitor titration curve determines the concentration of the enzyme. Combining it with the known rotation:ATP stoichiometry of V-ATPase and the assayed concentration of inorganic phosphate liberated by V-ATPase leads to an average rate of ~9.53 Hz of the 360 degrees rotation, which, according to the time-dependence of the activity, extrapolates to ~14.14 Hz for the beginning of the reaction. These are low limit estimates. To our knowledge this is the first report of the rotation rate in a V-ATPase that is not subjected to genetic or chemical modification and it is not fixed on a solid support, instead it is functioning in its native membrane environment.Special Issue: Structure, function, folding and assembly of membrane proteins -Insight from Biophysics.

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Section: Atpase Activity Assaymentioning

confidence: 93%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Estimating the rotation rate in the vacuolar proton-ATPase in native yeast vacuolar membranes

et al. 2012

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“…112 The disruption of pH homeostasis in v-H + -ATPase mutants showed lethality in various organisms. 114 In murine cardiomyocytes, ablation of ATP6ap2 selectively suppressed protein expression of the V O subunits of v-H + -ATPase resulting in loss of function for v-H + -ATPase leading to de-acidification of intracellular vesicles. 112 The (P)RR is essential along functional link with the v-H + -ATPase for cell survival and in early organ development.…”

Section: Implication Of (P)rrs In Pathologic Conditionsmentioning

confidence: 99%

Potential cross-talk between (pro)renin receptors and Wnt/frizzled receptors in cardiovascular and renal disorders

Balakumar

Jagadeesh

2011

Hypertens Res

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The renin-angiotensin system and Wnt/frizzled receptor signaling pathways are important in the development of essential organs, and their aberrant activation results in cardiovascular and renal pathologies. The (pro)renin receptor ((P)RR)-bound (pro)renin is enzymatically active generating angiotensin-II and activating mitogen-activated protein kinases, leading to cell proliferation and to upregulation of profibrotic genes expression, resulting in end-organ damage. The (P)RR does more than bind to (pro)renin, because it is functionally linked to the vacuolar-H + -ATPase (v-H + -ATPase) that regulates pH of cellular and intracellular vesicles, and to Wnt signaling. This signaling pathway is essential for cell survival, embryonic development and has had a role in various disease states as evidenced by mutation or genetic ablation of the (P)RR gene. This suggests two types of functions of (P)RRs, first one as a receptor for (pro)renin and second one as an accessory subunit of the v-H + -ATPase and a cofactor of the Wnt/Fz receptor complex. This review will discuss both of these functions of (P)RRs thereby giving new perspectives as to the roles of (P)RRs in cardiovascular and renal pathologies.

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“…The idea of the V-type ATPases took much more time to mature (see [3] for a review). The Vtype ATPases are now known to form an independent group of ion-transport ATPases using a molecular motor reminiscent of that found in the bacterial F-type ATPases.…”

mentioning

confidence: 99%

Half a century of ion-transport ATPases: the P- and V-type ATPases

Wuytack

2008

Pflugers Arch - Eur J Physiol

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This special issue focuses on two important types of ionmotive ATPases: P-type ATPases that are characterised by the formation of a phosphoprotein intermediate and V-type ATPases found in the diverse compartments belonging to the eukaryotic vacuolar system, which includes not only components of the secretory and endocytotic membrane system but also the plasma membrane.The 1940s and the early 1950s were of pivotal importance for the newly emerging field of electrophysiology. In the course of this decennium, physiologists witnessed the gradual development of the concept of active transport of inorganic ions in cells. It became at that time, partly by the use of radioisotopes, gradually but undeniably clear that biological membranes do not act as barriers impermeable to ions like Na + or K + but that instead there exists a continuous transmembrane exchange of ions, and hence, that in order to ensure a steady state, cells had to actively move Na + and K + against concentration gradients. It was soon realised that the thus generated transmembrane electrochemical ion gradient can be used to drive other ions or non-ionic compounds uphill and that it allows the generation of electrical activity in the form of action potentials. However, it was also clear that preserving this transmembrane gradient, in face of the ongoing drain imposed by the various ion movements, requires the continuous input of energy. It is not surprising that evolution has pioneered many different types of active transport systems to counter these leaks. But the question remained how can chemical energy be harnessed to catalyse a vectorial transmembrane transport of ions?It was Jens C. Skou in Denmark who, about 50 years ago in 1957, first pointed to an adenosine triphosphatase as the motor of this active transport system [1], a discovery that only 40 years later earned him the Nobel prize for Chemistry 1997: "for the first discovery of an ion-transporting enzyme, Na + , K + -ATPase" (see Nobel lecture at http://nobelprize.org/ nobel_prizes/chemistry/laureates/1997/skou-lecture.html and [2]).The 1960s represent the decennium of the Ca 2+ -transporting ATPases. First, the Ca 2+ transport ATPase from skeletal muscle sarcoplasmic reticulum (SERCA) and shortly thereafter that of erythrocyte plasma membrane (PMCA) joined the scene. The challenge became now to unravel the individual steps of the transport process. The phosphorylation of an aspartate residue in the ATPase was rapidly recognised as a necessary step in the catalytic cycle. The formation of this intermediate represents the hallmark of these ATPases, hence the name of this group of transporters, the P-type ATPases.But not all transport ATPases make use of a phosphoprotein intermediate. The idea of the V-type ATPases took much more time to mature (see [3] for a review). The Vtype ATPases are now known to form an independent group of ion-transport ATPases using a molecular motor reminiscent of that found in the bacterial F-type ATPases. It took indeed another 30 years after the discovery of the ...

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The V-type H+ ATPase: molecular structure and function,physiological roles and regulation

Cited by 562 publications

References 145 publications

Estimating the rotation rate in the vacuolar proton-ATPase in native yeast vacuolar membranes

Estimating the rotation rate in the vacuolar proton-ATPase in native yeast vacuolar membranes

Potential cross-talk between (pro)renin receptors and Wnt/frizzled receptors in cardiovascular and renal disorders

Half a century of ion-transport ATPases: the P- and V-type ATPases

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