Regulation of plasma membrane H(+)-ATPase in fungi and plants.

@article{Portillo2000RegulationOP,
  title={Regulation of plasma membrane H(+)-ATPase in fungi and plants.},
  author={Francisco Garc{\'i}a-del Portillo},
  journal={Biochimica et biophysica acta},
  year={2000},
  volume={1469 1},
  pages={
          31-42
        }
}
  • F. Portillo
  • Published 10 March 2000
  • Biology
  • Biochimica et biophysica acta
PLANT PLASMA MEMBRANE H+-ATPases: Powerhouses for Nutrient Uptake.
  • M. Palmgren
  • Biology
    Annual review of plant physiology and plant molecular biology
  • 2001
TLDR
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.
Regulation of plasma membrane H+-ATPase activity by the membrane environment
  • K. Kasamo
  • Biology, Chemistry
    Journal of Plant Research
  • 2004
The plant plasma membrane H+-ATPase is a proton pump which plays a central role in physiological functions such as nutrient uptake and intracellular pH regulation. This pump belongs to the P3-type
Structure, Mechanism, and Regulation of the Neurospora Plasma Membrane H+-ATPase
TLDR
An atomic homology model of the proton pump based on the 2.6 angstrom x-ray structure of the related Ca2+ pump from rabbit sarcoplasmic reticulum reveals the likely path of theproton through the membrane and shows that the nucleotide-binding domain rotates by ∼70° to deliver adenosine triphosphate to the phosphorylation site.
The Role of Plasma Membrane H + -ATPase in Salinity Stress of Plants
TLDR
Plants adapted to salinity maintain a relatively low concentration of Na+ in the cytosol achieved through the active exclusion of sodium ions in the apoplast and vacuole, and it is believed that plant plasma membrane H+-ATPase plays a major role in salt stress tolerance.
Evolutionary and Functional Analysis of a Chara Plasma Membrane H+-ATPase
TLDR
Results suggest that an auto-inhibition domain is located in the C-terminal domain, and that CHA1 is likely to have a different regulation mechanism compared to the yeast and land plant PM H+-ATPases.
Evolutionary appearance of the plasma membrane H+-ATPase containing a penultimate threonine in the bryophyte
TLDR
It is shown that the moss Physcomitrella patens, which is known as a model bryophyte, expresses both the penultimate Thr-containing H+-ATPase and non-pT H-atPase, and that pT H+, which is regulated by phosphorylation of itspenultimate Thr, most likely appeared for the first time in bryphyte.
Characterization of the Plasma Membrane H+-ATPase in the Liverwort Marchantia polymorpha1[W][OA]
TLDR
It is found that the pT H+-ATPase in thalli is phosphorylated in response to light, sucrose, and osmotic shock and that light-induced phosphorylation depends on photosynthesis.
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A plant plasma membrane proton-ATPase gene is regulated by development and environment and shows signs of a translational regulation.
TLDR
Analysis of translational and transcriptional fusions with gusA in transgenic plants suggests that the pma1 leader sequence might activate translation of the main open reading frame, even though the URF is translated by a large majority of the scanning ribosomes.
Evidence for a plasma membrane proton pump in phloem cells of higher plants.
TLDR
The hypothesis that a proton pump is present in phloem cells, possibly providing energy to drive plasma membrane cotransport systems required forphloem loading and translocation of photosynthates, is supported.
Metabolic Modulation of Transport Coupling Ratio in Yeast Plasma Membrane H+-ATPase (*)
TLDR
It is suggested that intrinsic uncoupling is an important mechanism for regulation of pump activity in yeast cells and the number of protons transported per ATP hydrolyzed is significantly increased after glucose activation.
Transcriptional regulation by glucose of the yeast PMA1 gene encoding the plasma membrane H+‐ATPase
TLDR
Examination of the pool of newly synthesized ATPase that accumulates in secretory vesicles en route to the cell surface in the temperature‐sensitive secretory mutant sec6‐4 suggests a model in which transcriptional regulation of the ATPase gene by glucose is mediated by TUF/RAP1.
Characterization of plasma membrane H+‐ATPase from salt‐tolerant yeast Candida versatilis
TLDR
No in vivo activation of H+‐ATPase by glucose metabolism was observed in C. versatilis cells and the activity was independent of the growth phase, like Z. rouxii and unlike S. cerevisiae cells.
Yeast plasma membrane ATPase is essential for growth and has homology with (Na+ + K+), K+- and Ca2+-ATPases
TLDR
The strong homology between the ammo-acid sequence encoded by PMA1 and those of (Na+ + K+), Na+-, K+- and Ca2+-ATPases is consistent with the notion that the family of cation pumps which form a phosphorylated intermediate evolved from a common ancestral ATPase.
A major isoform of the maize plasma membrane H(+)-ATPase: characterization and induction by auxin in coleoptiles.
TLDR
It is concluded that auxin-induced acidification in coleoptile segments most often occurs in the nonvascular tissue and is mediated, at least in part, by increased levels of MHA2.
Maturation of the yeast plasma membrane [H+]ATPase involves phosphorylation during intracellular transport
TLDR
This study shows that the plasma membrane [H+]ATPase of Saccharomyces cerevisiae is phosphorylated on multiple Ser and Thr residues in vivo and suggests that reversible, site-specific phosphorylation serves to adjust ATPase activity in response to nutritional signals.
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