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Activation of the plasma membrane H(+)-ATPase by acid stress: Antibodies as a tool to follow the phosphorylation status of the penultimate activating Thr

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Bobik, Krzysztof [UCL] Boutry, Marc [UCL] Duby, Geoffrey [UCL]

Tight regulation of the plasma membrane proton pump ATPase (H(+)-ATPase) is necessary for controlling the membrane potential that energizes secondary transporters. This regulation relies on the phosphorylation of the H(+)-ATPase penultimate residue, a theonine, and the subsequent binding of regulatory 14-3-3 proteins, which results in enzyme activation. Using phosphospecific antibodies directed against the phosphorylable Thr of either PMA2 (Plasma membrane H(+)-ATPase from N. plumbaginifolia) or PMA4, we showed that the kinetics and extent of phosphorylation differ between both isoforms according to the growth or environmental conditions like cold stress.(1) Here, we used phospho-specific antibodies to follow PMA2 Thr phosphorylation upon acidification of the cytosol by incubating N. tabacum BY2 cells with four different weak organic acids. Increased PMA2 phosphorylation was observed for three of them, thus highlighting the role of the H(+)-ATPase in cell pH homeostasis.

Document type Article de périodique (Journal article) – Article de recherche – Journal Article
Publication date 2010
Language Anglais
Journal information "Plant signaling & behavior" - Vol. 5, no. 6, p. 681-3 (2010)
Peer reviewed yes
e-issn 1559-2324
issn 1559-2316
Publication status Publié
Affiliation UCL - Autre
Links
  1. Bobik Krzysztof, Duby Geoffrey, Nizet Yannick, Vandermeeren Caroline, Stiernet Patrick, Kanczewska Justyna, Boutry Marc, Two widely expressed plasma membrane H+-ATPase isoforms of Nicotiana tabacum are differentially regulated by phosphorylation of their penultimate threonine : Differential regulation of H+-ATPases, 10.1111/j.1365-313x.2010.04147.x
  2. Palmgren Michael G, PLANTPLASMAMEMBRANEH+-ATPases: Powerhouses for Nutrient Uptake, 10.1146/annurev.arplant.52.1.817
  3. Duby Geoffrey, Boutry Marc, The plant plasma membrane proton pump ATPase: a highly regulated P-type ATPase with multiple physiological roles, 10.1007/s00424-008-0457-x
  4. Fuglsang Anja T., Visconti Sabina, Drumm Katrine, Jahn Thomas, Stensballe Allan, Mattei Benedetta, Jensen Ole N., Aducci Patrizia, Palmgren Michael G., Binding of 14-3-3 Protein to the Plasma Membrane H+-ATPase AHA2 Involves the Three C-terminal Residues Tyr946-Thr-Val and Requires Phosphorylation of Thr947, 10.1074/jbc.274.51.36774
  5. Maudoux Olivier, Batoko Henri, Oecking Claudia, Gevaert Kris, Vandekerckhove Joel, Boutry Marc, Morsomme Pierre, A Plant Plasma Membrane H+-ATPase Expressed in Yeast Is Activated by Phosphorylation at Its Penultimate Residue and Binding of 14-3-3 Regulatory Proteins in the Absence of Fusicoccin, 10.1074/jbc.m909690199
  6. Kanczewska J., Marco S., Vandermeeren C., Maudoux O., Rigaud J.-L., Boutry M., Activation of the plant plasma membrane H+-ATPase by phosphorylation and binding of 14-3-3 proteins converts a dimer into a hexamer, 10.1073/pnas.0504498102
  7. Ottmann Christian, Marco Sergio, Jaspert Nina, Marcon Caroline, Schauer Nicolas, Weyand Michael, Vandermeeren Caroline, Duby Geoffrey, Boutry Marc, Wittinghofer Alfred, Rigaud Jean-Louis, Oecking Claudia, Structure of a 14-3-3 Coordinated Hexamer of the Plant Plasma Membrane H+-ATPase by Combining X-Ray Crystallography and Electron Cryomicroscopy, 10.1016/j.molcel.2006.12.017
  8. Duby Geoffrey, Poreba Wojciech, Piotrowiak Dominik, Bobik Krzysztof, Derua Rita, Waelkens Etienne, Boutry Marc, Activation of Plant Plasma Membrane H+-ATPase by 14-3-3 Proteins Is Negatively Controlled by Two Phosphorylation Sites within the H+-ATPase C-terminal Region, 10.1074/jbc.m807311200
  9. Fuglsang A. T., Guo Y., Cuin T. A., Qiu Q., Song C., Kristiansen K. A., Bych K., Schulz A., Shabala S., Schumaker K. S., Palmgren M. G., Zhu J.-K., Arabidopsis Protein Kinase PKS5 Inhibits the Plasma Membrane H+-ATPase by Preventing Interaction with 14-3-3 Protein, 10.1105/tpc.105.035626
  10. Niittylä Totte, Fuglsang Anja T., Palmgren Michael G., Frommer Wolf B., Schulze Waltraud X., Temporal Analysis of Sucrose-induced Phosphorylation Changes in Plasma Membrane Proteins ofArabidopsis, 10.1074/mcp.m700164-mcp200
  11. Nuhse T. S., Phosphoproteomics of the Arabidopsis Plasma Membrane and a New Phosphorylation Site Database, 10.1105/tpc.104.023150
  12. Axelsen K. B., Venema K., Jahn T., Baunsgaard L., Palmgren M. G., Molecular Dissection of the C-Terminal Regulatory Domain of the Plant Plasma Membrane H+-ATPase AHA2:  Mapping of Residues that When Altered Give Rise to an Activated Enzyme†, 10.1021/bi982482l
  13. Speth Corinna, Jaspert Nina, Marcon Caroline, Oecking Claudia, Regulation of the plant plasma membrane H+-ATPase by its C-terminal domain: what do we know for sure?, 10.1016/j.ejcb.2009.10.015
  14. Moriau Luc, Michelet Baudouin, Bogaerts Pierre, Lambert Laurence, Michel Alain, Oufattole Mohammed, Boutry Marc, Expression analysis of two gene subfamilies encoding the plasma membrane H+-ATPase in Nicotiana plumbaginifolia reveals the major transport functions of this enzyme, 10.1046/j.1365-313x.1999.00495.x
Bibliographic reference Bobik, Krzysztof ; Boutry, Marc ; Duby, Geoffrey. Activation of the plasma membrane H(+)-ATPase by acid stress: Antibodies as a tool to follow the phosphorylation status of the penultimate activating Thr. In: Plant signaling & behavior, Vol. 5, no. 6, p. 681-3 (2010)
Permanent URL http://hdl.handle.net/2078.1/32153