Helmholtz Gemeinschaft

Search
Browse
Statistics
Feeds

The lipid head group is the key element for substrate recognition by the P4 ATPase ALA2: a phosphatidylserine flippase

[thumbnail of Original Article]
Preview
PDF (Original Article) - Requires a PDF viewer such as GSview, Xpdf or Adobe Acrobat Reader
8MB
[thumbnail of Supplementary Tables]
Preview
PDF (Supplementary Tables) - Requires a PDF viewer such as GSview, Xpdf or Adobe Acrobat Reader
188kB

Item Type:Article
Title:The lipid head group is the key element for substrate recognition by the P4 ATPase ALA2: a phosphatidylserine flippase
Creators Name:Theorin, L., Faxén, K., Sørensen, D.M., Migotti, R., Dittmar, G., Schiller, J., Daleke, D.L., Palmgren, M., López-Marqués, R.L. and Pomorski, T.G.
Abstract:Type IV P-type ATPases (P4 ATPases) are lipid flippases that catalyze phospholipid transport from the exoplasmic to the cytoplasmic leaflet of cellular membranes, but the mechanism by which they recognize and transport phospholipids through the lipid bilayer remains unknown. In the present study, we succeeded in purifying recombinant aminophospholipid ATPase 2 (ALA2), a member of the P4 ATPase subfamily in Arabidopsis thaliana, in complex with the ALA-interacting subunit 5 (ALIS5). The ATP hydrolytic activity of the ALA2–ALIS5 complex was stimulated in a highly specific manner by phosphatidylserine. Small changes in the stereochemistry or the functional groups of the phosphatidylserine head group affected enzymatic activity, whereas alteration in the length and composition of the acyl chains only had minor effects. Likewise, the enzymatic activity of the ALA2–ALIS5 complex was stimulated by both mono- and di-acyl phosphatidylserines. Taken together, the results identify the lipid head group as the key structural element for substrate recognition by the P4 ATPase.
Keywords:Arabidopsis thaliana, FLAG-Tag Purification, Lipid Flippase, Lysophospholipid, Membrane Protein Complex
Source:Biochemical Journal
ISSN:0264-6021
Publisher:Portland Press
Volume:476
Number:5
Page Range:783-794
Date:6 March 2019
Official Publication:https://doi.org/10.1042/BCJ20180891
PubMed:View item in PubMed

Repository Staff Only: item control page

Downloads

Downloads per month over past year

Open Access
MDC Library