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Receptor kinase-mediated control of primary active proton pumping at the plasma membrane
journal contribution
posted on 2023-05-18, 07:02 authored by Fuglsang, AT, Kristensen, A, Tracey Cuin, Schulze, WX, Persson, J, Thuesen, KH, Ytting, CK, Oehlenschlaeger, CB, Mahmood, K, Sondergaard, TE, Sergey ShabalaSergey Shabala, Palmgren, MGAcidification 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.
History
Publication title
The Plant JournalVolume
80Issue
6Pagination
951-964ISSN
0960-7412Department/School
Tasmanian Institute of Agriculture (TIA)Publisher
Blackwell Publishing LtdPlace of publication
9600 Garsington Rd, Oxford, England, Oxon, Ox4 2DgRights statement
Copyright 2014 John Wiley & Sons LtdRepository Status
- Restricted