Anionic phospholipids stimulate the proton pumping activity of the plant plasma membrane P-Type H\(^{+}\)-ATPase

  • 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 \(\textit {Arabidopsis thaliana}\) 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.

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Author:Laura C. PaweletzORCiDGND, Simon L. HoltbrüggeGND, Malina LöbGND, Dario De VecchisGND, Lars V. SchäferORCiDGND, Thomas Günther-PomorskiORCiDGND, Bo Højen JustesenGND
Parent Title (English):International journal of molecular sciences
Place of publication:Basel
Document Type:Article
Date of Publication (online):2024/02/28
Date of first Publication:2023/08/23
Publishing Institution:Ruhr-Universität Bochum, Universitätsbibliothek
Tag:Open Access Fonds
H\(^{+}\)-ATPase; lipid–protein interaction; liposome; molecular modeling; proton pump; reconstitution
Issue:17, Artikel 13106
First Page:13106-1
Last Page:13106-21
Article Processing Charge funded by the Deutsche Forschungsgemeinschaft (DFG) and the Open Access Publication Fund of Ruhr-Universität Bochum.
Institutes/Facilities:Lehrstuhl Biochemie II, Molekulare Biochemie
Dewey Decimal Classification:Naturwissenschaften und Mathematik / Chemie, Kristallographie, Mineralogie
open_access (DINI-Set):open_access
faculties:Fakultät für Chemie und Biochemie
Licence (English):License LogoCreative Commons - CC BY 4.0 - Attribution 4.0 International