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  • 1
    Electronic Resource
    Electronic Resource
    PLANT PLASMA MEMBRANE H+-ATPases: Powerhouses for Nutrient Uptake (2001)
    Palo Alto, Calif. : Annual Reviews
    Annual Review of Plant Physiology and Plant Molecular Biology 52 (2001), S. 817-845 
    Details
    ISSN: 1040-2519
    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
    Topics: Biology
    Notes: Abstract Most transport proteins in plant cells are energized by electrochemical gradients of protons across the plasma membrane. The formation of these gradients is due to the action of plasma membrane H+ pumps fuelled by ATP. The plasma membrane H+-ATPases share a membrane topography and general mechanism of action with other P-type ATPases, but differ in regulatory properties. Recent advances in the field include the identification of the complete H+-ATPase gene family in Arabidopsis, analysis of H+-ATPase function by the methods of reverse genetics, an improved understanding of the posttranslational regulation of pump activity by 14-3-3 proteins, novel insights into the H+ transport mechanism, and progress in structural biology. Furthermore, the elucidation of the three-dimensional structure of a related Ca2+ pump has implications for understanding of structure-function relationships for the plant plasma membrane H+-ATPase.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1146/annurev.arplant.52.1.817
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  • 2
    Electronic Resource
    Electronic Resource
    Regulation of plant plasma membrane H+-ATPase activity (1991)
    Oxford, UK : Blackwell Publishing Ltd
    Physiologia plantarum 83 (1991), S. 0 
    Details
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: The plant plasma membrane H+-ATPase plays a central role in plant physiology. This enzyme belongs to the P type family of cation-translocating pumps and generates the proton-motive force that drives nutrient uptake across the plasma membrane. It also determines the extracellular acidification associated with elongation growth. The activity of the plasma membrane H+-ATPase is rapidly altered after exposure of plant tissues to plant growth factors such as plant hormones, light and pathogens. However, very little is known about the mechanisms that regulate plasma membrane H+-ATPase activity in the intact cell. The recent identification of an auto-inhibitory domain in the C-terminus of the plant plasma membrane H+-ATPase implies that there are several possible means by which the enzyme could be regulated. The inhibitory interaction between the inhibitory domain and the catalytic site and/or a proton binding site may thus be regulated by a variety of means, such as the binding of effector molecules, phosphorylation, partial proteolysis, or removal of the inhibitory domain at the gene level. In addition, proton pumping across the plasma membrane could be regulated by changes in the transcriptional activity of H+-ATPase genes or by differential expression of pump isoforms varying in their C-terminal domain.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1399-3054.1991.tb02159.x
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  • 3
    Electronic Resource
    Electronic Resource
    Substrate stabilization of lysophosphatidylcholine-solubilized plasma membrane H+-ATPase from oat roots (1988)
    Oxford, UK : Blackwell Publishing Ltd
    Physiologia plantarum 74 (1988), S. 0 
    Details
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Plasma membrane vesicles with H+-ATPase activity were purified from 8-day-old oat (Avena sativa L. cv. Brighton) roots using an aqueous polymer two-phase system. Of several detergents tested, only lysophosphatidylcholine solubilized the H+-ATPase in an active form. Solubilization of the H+-ATPase with lysophosphatidylcholine was possible in the absence of glycerol, but the ATPase activity decreased about 4–5 times as rapidly in the absence as in the presence of 30% (w/v) glycerol. The solubilized enzyme was further stabilized by ATP and protons. Addition of 1 mM ATP to the plasma membranes halted inactivation of the H+-ATPase. Even in the absence of polyol compounds and ATP, the enzyme was stable for hours at relatively low pH with an optimum around pH 6.7 at room temperature. The curve for the stability of soluble H+-ATPase as a function of pH closely resembles the pH curve for the activity of the H+-ATPase. This suggests that binding of protons to transport sites may stabilize the soluble H+-ATPase in an enzymatically active form.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1399-3054.1988.tb04935.x
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  • 4
    Electronic Resource
    Electronic Resource
    Two plant Ca2+ pumps expressed in stomatal guard cells show opposite expression patterns during cold stress (2005)
    Oxford, UK; Malden, USA : Munksgaard International Publishers
    Physiologia plantarum 124 (2005), S. 0 
    Details
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Guard cells respond to cold and other stimuli with an oscillating Ca2+ signal, causing an opening or closing of the stomatal pore. However, the molecular basis for the regulation of Ca2+ transients in guard cells has so far not been elucidated. We have localized the expression of two closely related Ca2+-ATPases, ACA8 and ACA10, to guard cells in Arabidopsis. Whereas ACA8 expression was limited to guard cells and vascular tissues, ACA10 was found to be ubiquitously expressed. Upon cold treatment, the expression of ACA8 was found to be upregulated while that of ACA10 was downregulated. This finding was supported by the presence of the cold responsive C-repeat/dehydration-responsive element motif in the ACA8 promoter sequence.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1399-3054.2005.00512.x
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  • 5
    Electronic Resource
    Electronic Resource
    Crystal structure of the plasma membrane proton pump (2007)
    [s.l.] : Nature Publishing Group
    Nature 450 (2007), S. 1111-1114 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] A prerequisite for life is the ability to maintain electrochemical imbalances across biomembranes. In all eukaryotes the plasma membrane potential and secondary transport systems are energized by the activity of P-type ATPase membrane proteins: H+-ATPase (the proton pump) in ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/nature06417
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  • 6
    Electronic Resource
    Electronic Resource
    Modulation of plasma membrane H+-ATPase from oat roots by lysophosphatidylcholine, free fatty acids and phospholipase A2 (1988)
    Oxford, UK : Blackwell Publishing Ltd
    Physiologia plantarum 74 (1988), S. 0 
    Details
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Plasma membrane vesicles were purified from 8-day-old oat (Avena sativa L. cv. Brighton) roots in an aqueous polymer two-phase system. The plasma membranes possessed high specific ATPase activity [ca 4 μmol P1 (mg protein)−1 min−1 at 37°C]. Addition of lysophosphatidylcholine (lyso-PC) produced a 2–3 fold activation of the plasma membrane ATPase, an effect due both to exposure of latent ATP binding sites and to a true activation of the enzyme. Lipid activation increased the affinity for ATP and caused a shift of the pH optimum of the H+ -ATPase activity to 6.75 as compared to pH 6.45 for the negative H+-ATPase. Activation was dependent on the chain length of the acyl group of the lyso-PC, with maximal activition obtained by palmitoyl lyso-PC. Free fatty acids also activated the membrane-bound H+-ATPase. This activation was also dependent on chain length and to the degree of unsaturation, with linolenic and arachidonic acid as the most efficient fatty acids. Exogenously added PC was hydrolyzed to lyso-PC and free fatty acids by an enzyme in the plasma membrane preparation, presumably of the phospholipase A type. Both lyso-PC and free fatty acids are products of phospholipase A2 (EC 3.1.1.4) action, and addition of phospholipase A2 from animal sources increased the H+-ATPase activity within seconds. Interaction with lipids and fatty acids could thus be part of the regulatory system for H+-ATPase activity in vivo, and the endogenous phospholipase may be involved in the regulation of the H+-ATPase activity in the plasma membranne.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1399-3054.1988.tb04934.x
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  • 7
    Electronic Resource
    Electronic Resource
    Evolution of Substrate Specificities in the P-Type ATPase Superfamily (1998)
    Springer
    Journal of molecular evolution 46 (1998), S. 84-101 
    Details
    ISSN: 1432-1432
    Keywords: Key words: Na+— K+— Cu2+— H+— Mg2+— Cd2+— Phospholipid translocases
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract. P-type ATPases make up a large superfamily of ATP-driven pumps involved in the transmembrane transport of charged substrates. We have performed an analysis of conserved core sequences in 159 P-type ATPases. The various ATPases group together in five major branches according to substrate specificity, and not according to the evolutionary relationship of the parental species, indicating that invention of new substrate specificities is accompanied by abrupt changes in the rate of sequence evolution. A hitherto-unrecognized family of P-type ATPases has been identified that is expected to be represented in all the major phyla of eukarya.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/PL00006286
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  • 8
    Electronic Resource
    Electronic Resource
    Deciphering the role of 14-3-3 proteins (1998)
    Springer
    Experimental biology online 3 (1998), S. 1-17 
    Details
    ISSN: 1430-3418
    Keywords: Binding motif ; H+-ATPase ; Plasma membrane ; 14-3-3 Protein ; Protein kinase C ; Modulator ; Raf-1 ; Signal transduction
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract 14-3-3 Proteins are found to bind to a growing number of eukaryotic proteins and evidence is accumulating that 14-3-3 proteins serve as modulators of enzyme activity. Several 14-3-3 protein recognition motifs have been identified and an increasing number of target proteins have been found to contain more than one binding site for a 14-3-3 protein. It is thus possible that 14-3-3 dimers function as clamps that simultaneously bind to two motifs within a single binding partner. Phosphorylation of a number of binding motifs has been shown to increase the affinity for 14-3-3 proteins but other mechanisms also regulate the association. It has recently been demonstrated that fusicoccin induces a tight association between 14-3-3 proteins and the plant plasma membrane H+-ATPase. Phorbol esters and other hydrophobic molecules may have a similar effect on the association between 14-3-3 proteins and specific binding partners.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s00898-998-0004-4
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  • 9
    Electronic Resource
    Electronic Resource
    Capturing of host DNA by a plant retroelement: Bs1 encodes plasma membrane H+-ATPase domains (1994)
    Springer
    Plant molecular biology 25 (1994), S. 137-140 
    Details
    ISSN: 1573-5028
    Keywords: DNA acquisition ; retrotransposon ; retrovirus ; Zea mays
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The recently identified maize retroelement Bs1 encodes domains of the plasma membrane H+-ATPase. This is the first example of host DNA captured by a plant retroelement and resembles the acquisition of oncogenes by vertebrate retroviruses. The ability to capture sequences from its host provides plant retroelements with a mechanism to alter gene structure which could be important for evolutionary adaptive change.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00023232
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  • 10
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    A lipid switch unlocks Parkinson’s disease-associated ATP13A2 (2015)
    National Academy of Sciences
    Details
    Publication Date: 2015-07-01
    Description: ATP13A2 is a lysosomal P-type transport ATPase that has been implicated in Kufor–Rakeb syndrome and Parkinson’s disease (PD), providing protection against α-synuclein, Mn2+, and Zn2+ toxicity in various model systems. So far, the molecular function and regulation of ATP13A2 remains undetermined. Here, we demonstrate that ATP13A2 contains a unique N-terminal hydrophobic extension that lies on the cytosolic membrane surface of the lysosome, where it interacts with the lysosomal signaling lipids phosphatidic acid (PA) and phosphatidylinositol(3,5)bisphosphate [PI(3,5)P2]. We further demonstrate that ATP13A2 accumulates in an inactive autophosphorylated state and that PA and PI(3,5)P2 stimulate the autophosphorylation of ATP13A2. In a cellular model of PD, only catalytically active ATP13A2 offers cellular protection against rotenone-induced mitochondrial stress, which relies on the availability of PA and PI(3,5)P2. Thus, the N-terminal binding of PA and PI(3,5)P2 emerges as a key to unlock the activity of ATP13A2, which may offer a therapeutic strategy to activate ATP13A2 and thereby reduce α-synuclein toxicity or mitochondrial stress in PD or related disorders.
    Print ISSN: 0027-8424
    Electronic ISSN: 1091-6490
    Topics: Biology , Medicine , Natural Sciences in General
    Published by National Academy of Sciences
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