pH modulates interaction of 14-3-3 proteins with pollen plasma membrane H+ ATPases independently from phosphorylation.

Autor:	Pertl-Obermeyer H; Membrane Biophysics, Department of Biosciences, University of Salzburg, Billrothstr. 11, 5020 Salzburg, Austria.; MorphoPhysics, Department of Chemistry and Physics of Materials, University of Salzburg, Jakob-Haringer-Str. 2a, 5020 Salzburg, Austria., Gimeno A; Membrane Biophysics, Department of Biosciences, University of Salzburg, Billrothstr. 11, 5020 Salzburg, Austria., Kuchler V; Membrane Biophysics, Department of Biosciences, University of Salzburg, Billrothstr. 11, 5020 Salzburg, Austria., Servili E; Membrane Biophysics, Department of Biosciences, University of Salzburg, Billrothstr. 11, 5020 Salzburg, Austria.; Inst. Recherche Experimentale & Clinique, University of Louvain, Ave. Hippocrate, Woluwe-Saint Lambert, Belgium., Huang S; Membrane Biophysics, Department of Biosciences, University of Salzburg, Billrothstr. 11, 5020 Salzburg, Austria.; Southern University of Science and Technology, Shenzen, PR China., Fang H; Membrane Biophysics, Department of Biosciences, University of Salzburg, Billrothstr. 11, 5020 Salzburg, Austria.; Spinal Chord Injury & Tissue Regeneration Centre, Paracelsus Medical University, Strubergasse, Salzburg, Austria., Lang V; Membrane Biophysics, Department of Biosciences, University of Salzburg, Billrothstr. 11, 5020 Salzburg, Austria.; STRATEC GmbH, Sonystraße 20, Anif, Austria., Sydow K; Membrane Biophysics, Department of Biosciences, University of Salzburg, Billrothstr. 11, 5020 Salzburg, Austria., Pöckl M; Membrane Biophysics, Department of Biosciences, University of Salzburg, Billrothstr. 11, 5020 Salzburg, Austria., Schulze WX; Plant Systems Biology, University of Hohenheim, Garbenstraße 30, 70599 Stuttgart, Germany., Obermeyer G; Membrane Biophysics, Department of Biosciences, University of Salzburg, Billrothstr. 11, 5020 Salzburg, Austria.
Jazyk:	angličtina
Zdroj:	Journal of experimental botany [J Exp Bot] 2022 Jan 05; Vol. 73 (1), pp. 168-181.
DOI:	10.1093/jxb/erab387
Abstrakt:	Pollen grains transport the sperm cells through the style tissue via a fast-growing pollen tube to the ovaries where fertilization takes place. Pollen tube growth requires a precisely regulated network of cellular as well as molecular events including the activity of the plasma membrane H+ ATPase, which is known to be regulated by reversible protein phosphorylation and subsequent binding of 14-3-3 isoforms. Immunodetection of the phosphorylated penultimate threonine residue of the pollen plasma membrane H+ ATPase (LilHA1) of Lilium longiflorum pollen revealed a sudden increase in phosphorylation with the start of pollen tube growth. In addition to phosphorylation, pH modulated the binding of 14-3-3 isoforms to the regulatory domain of the H+ ATPase, whereas metabolic components had only small effects on 14-3-3 binding, as tested with in vitro assays using recombinant 14-3-3 isoforms and phosphomimicking substitutions of the threonine residue. Consequently, local H+ influxes and effluxes as well as pH gradients in the pollen tube tip are generated by localized regulation of the H+ ATPase activity rather than by heterogeneous localized distribution in the plasma membrane. (© The Author(s) 2021. Published by Oxford University Press on behalf of the Society for Experimental Biology. All rights reserved. For permissions, please email: journals.permissions@oup.com.)
Databáze:	MEDLINE
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