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Plant J. 2014 Dec;80(6):951-64. doi: 10.1111/tpj.12680. Epub 2014 Oct 25.

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

Author information

1
Department of Plant and Environmental Science, Center for Membrane Pumps in Cells and Disease - PUMPKIN, Danish National Research Foundation, University of Copenhagen, DK-1871, Frederiksberg, Denmark.

Abstract

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.

KEYWORDS:

H+ pump; LRR kinase; apoplastic pH; cell elongation; peptide signalling

PMID:
25267325
DOI:
10.1111/tpj.12680
[Indexed for MEDLINE]
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