Potassium as an intrinsic uncoupler of the plasma membrane H+-ATPase

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Potassium as an intrinsic uncoupler of the plasma membrane H+-ATPase. / Palmgren, Michael Broberg; Buch-Pedersen, Morten Jeppe.

2006.

Research output: Contribution to conference › Conference abstract for conference › Research › peer-review

Harvard

Palmgren, MB & Buch-Pedersen, MJ 2006, 'Potassium as an intrinsic uncoupler of the plasma membrane H+-ATPase'.

APA

Palmgren, M. B., & Buch-Pedersen, M. J. (2006). Potassium as an intrinsic uncoupler of the plasma membrane H+-ATPase.

Vancouver

Palmgren MB, Buch-Pedersen MJ. Potassium as an intrinsic uncoupler of the plasma membrane H+-ATPase. 2006.

Author

Palmgren, Michael Broberg ; Buch-Pedersen, Morten Jeppe. / Potassium as an intrinsic uncoupler of the plasma membrane H+-ATPase.

Bibtex

@conference{0a897c73b49d4b11b9c190f9fa36297e,
title = "Potassium as an intrinsic uncoupler of the plasma membrane H+-ATPase",
abstract = "The plant plasma membrane proton pump (H(+)-ATPase) is stimulated by potassium, but it has remained unclear whether potassium is actually transported by the pump or whether it serves other roles. We now show that K(+) is bound to the proton pump at a site involving Asp(617) in the cytoplasmic phosphorylation domain, from where it is unlikely to be transported. Binding of K(+) to this site can induce dephosphorylation of the phosphorylated E(1)P reaction cycle intermediate by a mechanism involving Glu(184) in the conserved TGES motif of the pump actuator domain. Our data identify K(+) as an intrinsic uncoupler of the proton pump and suggest a mechanism for control of the H(+)/ATP coupling ratio. K(+)-induced dephosphorylation of E(1)P may serve regulatory purposes and play a role in negative regulation of the transmembrane electrochemical gradient under cellular conditions where E(1)P is accumulating.",
author = "Palmgren, {Michael Broberg} and Buch-Pedersen, {Morten Jeppe}",
year = "2006",
language = "English",

}

RIS

TY - ABST

T1 - Potassium as an intrinsic uncoupler of the plasma membrane H+-ATPase

AU - Palmgren, Michael Broberg

AU - Buch-Pedersen, Morten Jeppe

PY - 2006

Y1 - 2006

N2 - The plant plasma membrane proton pump (H(+)-ATPase) is stimulated by potassium, but it has remained unclear whether potassium is actually transported by the pump or whether it serves other roles. We now show that K(+) is bound to the proton pump at a site involving Asp(617) in the cytoplasmic phosphorylation domain, from where it is unlikely to be transported. Binding of K(+) to this site can induce dephosphorylation of the phosphorylated E(1)P reaction cycle intermediate by a mechanism involving Glu(184) in the conserved TGES motif of the pump actuator domain. Our data identify K(+) as an intrinsic uncoupler of the proton pump and suggest a mechanism for control of the H(+)/ATP coupling ratio. K(+)-induced dephosphorylation of E(1)P may serve regulatory purposes and play a role in negative regulation of the transmembrane electrochemical gradient under cellular conditions where E(1)P is accumulating.

AB - The plant plasma membrane proton pump (H(+)-ATPase) is stimulated by potassium, but it has remained unclear whether potassium is actually transported by the pump or whether it serves other roles. We now show that K(+) is bound to the proton pump at a site involving Asp(617) in the cytoplasmic phosphorylation domain, from where it is unlikely to be transported. Binding of K(+) to this site can induce dephosphorylation of the phosphorylated E(1)P reaction cycle intermediate by a mechanism involving Glu(184) in the conserved TGES motif of the pump actuator domain. Our data identify K(+) as an intrinsic uncoupler of the proton pump and suggest a mechanism for control of the H(+)/ATP coupling ratio. K(+)-induced dephosphorylation of E(1)P may serve regulatory purposes and play a role in negative regulation of the transmembrane electrochemical gradient under cellular conditions where E(1)P is accumulating.

UR - https://curis.ku.dk/portal/en/publications/potassium-as-an-intrinsic-uncoupler-of-the-plasma-membrane-hatpase(9412e810-a1c1-11dd-b6ae-000ea68e967b).html

M3 - Conference abstract for conference

ER -

ID: 304684402