Receptor kinase‐mediated control of primary active proton pumping at the plasma membrane

Acidification of the cell wall space outside the plasma membrane is required for plant growth and is the result of proton extrusion by the plasma membrane‐localized H⁺‐ATPases. Here we show that the major plasma membrane proton pumps in Arabidopsis, AHA1 and AHA2, interact directly in vitro and in p...

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Published in:The Plant journal : for cell and molecular biology Vol. 80; no. 6; pp. 951 - 964
Main Authors: Fuglsang, Anja T, Kristensen, Astrid, Cuin, Tracey A, Schulze, Waltraud X, Persson, Jörgen, Thuesen, Kristina H, Ytting, Cecilie K, Oehlenschlæger, Christian B, Mahmood, Khalid, Sondergaard, Teis E, Shabala, Sergey, Palmgren, Michael G
Format: Journal Article
Language:English
Published: England Blackwell Scientific Publishers and BIOS Scientific Publishers in association with the Society for Experimental Biology 01-12-2014
Blackwell Publishing Ltd
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Summary:Acidification of the cell wall space outside the plasma membrane is required for plant growth and is the result of proton extrusion by the plasma membrane‐localized H⁺‐ATPases. Here we show that the major plasma membrane proton pumps in Arabidopsis, AHA1 and AHA2, interact directly in vitro and in planta with PSY1R, a receptor kinase of the plasma membrane that serves as a receptor for the peptide growth hormone PSY1. The intracellular protein kinase domain of PSY1R phosphorylates AHA2/AHA1 at Thr‐881, situated in the autoinhibitory region I of the C‐terminal domain. When expressed in a yeast heterologous expression system, the introduction of a negative charge at this position caused pump activation. Application of PSY1 to plant seedlings induced rapid in planta phosphorylation at Thr‐881, concomitant with an instantaneous increase in proton efflux from roots. The direct interaction between AHA2 and PSY1R observed might provide a general paradigm for regulation of plasma membrane proton transport by receptor kinases.
Bibliography:http://dx.doi.org/10.1111/tpj.12680
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ISSN:0960-7412
1365-313X
DOI:10.1111/tpj.12680