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

Research output: Contribution to conference › Conference abstract for conference › Research

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

2006. Abstract from Plant Transporters Meeting, Wye, United Kingdom.

Research output: Contribution to conference › Conference abstract for conference › Research

Harvard

Palmgren, MG & Buch-Pedersen, MJ 2006, 'Potassium as an intrinsic uncoupler of the plasma membrane H+-ATPase', Plant Transporters Meeting, Wye, United Kingdom, 04/09/2006 - 06/09/2006.

APA

Palmgren, M. G., & Buch-Pedersen, M. J. (2006). Potassium as an intrinsic uncoupler of the plasma membrane H+-ATPase. Abstract from Plant Transporters Meeting, Wye, United Kingdom.

Vancouver

Palmgren MG, Buch-Pedersen MJ. Potassium as an intrinsic uncoupler of the plasma membrane H+-ATPase. 2006. Abstract from Plant Transporters Meeting, Wye, United Kingdom.

Author

Palmgren, Michael Gjedde ; Buch-Pedersen, Morten Jeppe. / Potassium as an intrinsic uncoupler of the plasma membrane H+-ATPase. Abstract from Plant Transporters Meeting, Wye, United Kingdom.1 p.

Bibtex

@conference{9412e810a1c111ddb6ae000ea68e967b,
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 Gjedde} and Buch-Pedersen, {Morten Jeppe}",
note = "Sider: 7; null ; Conference date: 04-09-2006 Through 06-09-2006",
year = "2006",
language = "English",

}

RIS

TY - ABST

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

AU - Palmgren, Michael Gjedde

AU - Buch-Pedersen, Morten Jeppe

N1 - Sider: 7

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.

M3 - Conference abstract for conference

Y2 - 4 September 2006 through 6 September 2006

ER -

ID: 8048473