Anionic Phospholipids Stimulate the Proton Pumping Activity of the Plant Plasma Membrane P-Type H+-ATPase

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Anionic Phospholipids Stimulate the Proton Pumping Activity of the Plant Plasma Membrane P-Type H+-ATPase. / Paweletz, Laura C.; Holtbrügge, Simon L.; Löb, Malina; De Vecchis, Dario; Schäfer, Lars V.; Günther Pomorski, Thomas; Justesen, Bo Højen.

In: International Journal of Molecular Sciences, Vol. 24, No. 17, 13106, 2023.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Paweletz, LC, Holtbrügge, SL, Löb, M, De Vecchis, D, Schäfer, LV, Günther Pomorski, T & Justesen, BH 2023, 'Anionic Phospholipids Stimulate the Proton Pumping Activity of the Plant Plasma Membrane P-Type H+-ATPase', International Journal of Molecular Sciences, vol. 24, no. 17, 13106. https://doi.org/10.3390/ijms241713106

APA

Paweletz, L. C., Holtbrügge, S. L., Löb, M., De Vecchis, D., Schäfer, L. V., Günther Pomorski, T., & Justesen, B. H. (2023). Anionic Phospholipids Stimulate the Proton Pumping Activity of the Plant Plasma Membrane P-Type H+-ATPase. International Journal of Molecular Sciences, 24(17), [13106]. https://doi.org/10.3390/ijms241713106

Vancouver

Paweletz LC, Holtbrügge SL, Löb M, De Vecchis D, Schäfer LV, Günther Pomorski T et al. Anionic Phospholipids Stimulate the Proton Pumping Activity of the Plant Plasma Membrane P-Type H+-ATPase. International Journal of Molecular Sciences. 2023;24(17). 13106. https://doi.org/10.3390/ijms241713106

Author

Paweletz, Laura C. ; Holtbrügge, Simon L. ; Löb, Malina ; De Vecchis, Dario ; Schäfer, Lars V. ; Günther Pomorski, Thomas ; Justesen, Bo Højen. / Anionic Phospholipids Stimulate the Proton Pumping Activity of the Plant Plasma Membrane P-Type H+-ATPase. In: International Journal of Molecular Sciences. 2023 ; Vol. 24, No. 17.

Bibtex

@article{3a76f18a337148dca959d08a69d655a8,
title = "Anionic Phospholipids Stimulate the Proton Pumping Activity of the Plant Plasma Membrane P-Type H+-ATPase",
abstract = "The activity of membrane proteins depends strongly on the surrounding lipid environment. Here, we characterize the lipid stimulation of the plant plasma membrane H+-ATPase Arabidopsis thaliana H+-ATPase isoform 2 (AHA2) upon purification and reconstitution into liposomes of defined lipid compositions. We show that the proton pumping activity of AHA2 is stimulated by anionic phospholipids, especially by phosphatidylserine. This activation was independent of the cytoplasmic C-terminal regulatory domain of the pump. Molecular dynamics simulations revealed several preferential contact sites for anionic phospholipids in the transmembrane domain of AHA2. These contact sites are partially conserved in functionally different P-type ATPases from different organisms, suggesting a general regulation mechanism by the membrane lipid environment. Our findings highlight the fact that anionic lipids play an important role in the control of H+-ATPase activity.",
keywords = "H-ATPase, lipid–protein interaction, liposome, molecular modeling, proton pump, reconstitution",
author = "Paweletz, {Laura C.} and Holtbr{\"u}gge, {Simon L.} and Malina L{\"o}b and {De Vecchis}, Dario and Sch{\"a}fer, {Lars V.} and {G{\"u}nther Pomorski}, Thomas and Justesen, {Bo H{\o}jen}",
note = "Publisher Copyright: {\textcopyright} 2023 by the authors.",
year = "2023",
doi = "10.3390/ijms241713106",
language = "English",
volume = "24",
journal = "International Journal of Molecular Sciences (Online)",
issn = "1661-6596",
publisher = "MDPI AG",
number = "17",

}

RIS

TY - JOUR

T1 - Anionic Phospholipids Stimulate the Proton Pumping Activity of the Plant Plasma Membrane P-Type H+-ATPase

AU - Paweletz, Laura C.

AU - Holtbrügge, Simon L.

AU - Löb, Malina

AU - De Vecchis, Dario

AU - Schäfer, Lars V.

AU - Günther Pomorski, Thomas

AU - Justesen, Bo Højen

N1 - Publisher Copyright: © 2023 by the authors.

PY - 2023

Y1 - 2023

N2 - The activity of membrane proteins depends strongly on the surrounding lipid environment. Here, we characterize the lipid stimulation of the plant plasma membrane H+-ATPase Arabidopsis thaliana H+-ATPase isoform 2 (AHA2) upon purification and reconstitution into liposomes of defined lipid compositions. We show that the proton pumping activity of AHA2 is stimulated by anionic phospholipids, especially by phosphatidylserine. This activation was independent of the cytoplasmic C-terminal regulatory domain of the pump. Molecular dynamics simulations revealed several preferential contact sites for anionic phospholipids in the transmembrane domain of AHA2. These contact sites are partially conserved in functionally different P-type ATPases from different organisms, suggesting a general regulation mechanism by the membrane lipid environment. Our findings highlight the fact that anionic lipids play an important role in the control of H+-ATPase activity.

AB - The activity of membrane proteins depends strongly on the surrounding lipid environment. Here, we characterize the lipid stimulation of the plant plasma membrane H+-ATPase Arabidopsis thaliana H+-ATPase isoform 2 (AHA2) upon purification and reconstitution into liposomes of defined lipid compositions. We show that the proton pumping activity of AHA2 is stimulated by anionic phospholipids, especially by phosphatidylserine. This activation was independent of the cytoplasmic C-terminal regulatory domain of the pump. Molecular dynamics simulations revealed several preferential contact sites for anionic phospholipids in the transmembrane domain of AHA2. These contact sites are partially conserved in functionally different P-type ATPases from different organisms, suggesting a general regulation mechanism by the membrane lipid environment. Our findings highlight the fact that anionic lipids play an important role in the control of H+-ATPase activity.

KW - H-ATPase

KW - lipid–protein interaction

KW - liposome

KW - molecular modeling

KW - proton pump

KW - reconstitution

U2 - 10.3390/ijms241713106

DO - 10.3390/ijms241713106

M3 - Journal article

C2 - 37685912

AN - SCOPUS:85170278012

VL - 24

JO - International Journal of Molecular Sciences (Online)

JF - International Journal of Molecular Sciences (Online)

SN - 1661-6596

IS - 17

M1 - 13106

ER -

ID: 382550208