Receptor kinase‐mediated control of primary active proton pumping at the plasma membrane. (25th October 2014)

• Record Type: Journal Article
• 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.
• Is Part Of: Plant journal. Volume 80:Number 6(2014:Dec.)
• Page Start: 951
• Page End: 964
• Publication Date: 2014-10-25
• Subjects: Plant molecular biology -- Periodicals; Plant cells and tissues -- Periodicals; Botany -- Periodicals; 580
• DOI: 10.1111/tpj.12680
• Languages: English
• ISSNs: 0960-7412

Abstract

<abstract abstract-type="main" id="tpj12680-abs-0001"> <title>Summary</title> <p>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 <italic>in vitro</italic> and <italic>in planta</italic> 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 <italic>in planta</italic> 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.</p> </abstract>