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Receptor kinase‐mediated control of primary active proton pumping at the plasma membrane
Author(s) -
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.
Publication year - 2014
Publication title -
the plant journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.058
H-Index - 269
eISSN - 1365-313X
pISSN - 0960-7412
DOI - 10.1111/tpj.12680
Subject(s) - microbiology and biotechnology , protein kinase a , kinase , phosphorylation , intracellular , protein kinase domain , proton pump , biophysics , membrane , chemistry , biology , biochemistry , atpase , enzyme , mutant , gene
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 + ‐ ATP ases. Here we show that the major plasma membrane proton pumps in A rabidopsis, AHA 1 and AHA 2, interact directly in vitro and in planta with PSY 1R, a receptor kinase of the plasma membrane that serves as a receptor for the peptide growth hormone PSY 1. The intracellular protein kinase domain of PSY 1 R phosphorylates AHA 2/ AHA 1 at T hr‐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 PSY 1 to plant seedlings induced rapid in planta phosphorylation at T hr‐881, concomitant with an instantaneous increase in proton efflux from roots. The direct interaction between AHA 2 and PSY 1 R observed might provide a general paradigm for regulation of plasma membrane proton transport by receptor kinases.