Receptor kinase-mediated control of primary active proton pumping at the plasma membrane
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Receptor kinase-mediated control of primary active proton pumping at the plasma membrane. / Fuglsang, Anja Thoe; Kristensen, Astrid; Cuin, Tracey A.; Schulze, Waltraud X.; Persson, Rolf Jörgen; Thuesen, Kristina Heinsbæk; Ytting, Cecilie Karkov; Oehlenschlæger, Christian Berg; Mahmood, Khalid; Søndergaard, Teis Esben; Shabala, Sergey; Palmgren, Michael Broberg.
In: Plant Journal, Vol. 80, No. 6, 2014, p. 951-964.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - Receptor kinase-mediated control of primary active proton pumping at the plasma membrane
AU - Fuglsang, Anja Thoe
AU - Kristensen, Astrid
AU - Cuin, Tracey A.
AU - Schulze, Waltraud X.
AU - Persson, Rolf Jörgen
AU - Thuesen, Kristina Heinsbæk
AU - Ytting, Cecilie Karkov
AU - Oehlenschlæger, Christian Berg
AU - Mahmood, Khalid
AU - Søndergaard, Teis Esben
AU - Shabala, Sergey
AU - Palmgren, Michael Broberg
PY - 2014
Y1 - 2014
N2 - 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.
AB - 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.
KW - apoplastic pH
KW - cell elongation
KW - H pump
KW - LRR kinase
KW - peptide signalling
U2 - 10.1111/tpj.12680
DO - 10.1111/tpj.12680
M3 - Journal article
C2 - 25267325
AN - SCOPUS:84916638439
VL - 80
SP - 951
EP - 964
JO - Plant Journal
JF - Plant Journal
SN - 0960-7412
IS - 6
ER -
ID: 131360436