(c) p40PX-GFP localizes to the cytoplasm and to membranes of the food vacuole (labelled with anti-CRT) and apicoplast (labelled with anti-ACP). STEVORss-p40PX-GFP localizes to the PV in P. falciparum-infected erythrocytes, as shown by co-localization with anti-EXP2, and not in the ER, which was labelled with anti-PMV. If PI(3)P was located within the ER, this chimera would be expected to remain within the ER via p40PX binding. Fusion to an ER-retention signal (STEVORss-p40PX-GFPSDEL) retains the protein in ER, co-localization with anti-ERC. Scale bar, 5 mm.
(d) Localization of Hrs-GFP to the cytoplasm and membranes of food vacuole (labelled anti-CRT) and apicoplast (labelled anti-ACP). STEVORss-Hrs-GFP localizes to the ER as shown by co-localization with anti-ERC; however, mutation of residues necessary for lipid binding in both Hrs FYVE fingers (STEVORss-HrsC215S-GFP) does not abrogate ER localization, demonstrating PI(3)P-independent retention in ER. Addition of ER retention signal (STEVORss-Hrs-GFPSDEL) also causes ER localization. Scale bar, 5 mm.
Boddey JA, O'Neill MT, Lopaticki S, Carvalho TG, Hodder AN, Nebl T, Wawra S,
van West P, Ebrahimzadeh Z, Richard D, Flemming S, Spielmann T, Przyborski J,
Babon JJ, Cowman AF. Export of malaria proteins requires co-translational
processing of the PEXEL motif independent of phosphatidylinositol-3-phosphate
binding. Nat Commun. 2016 Feb 1;7:10470.
Other associated proteins
|PF3D7_0208500||acyl carrier protein|
|PF3D7_0709000||chloroquine resistance transporter|
|PF3D7_1108600||endoplasmic reticulum-resident calcium binding protein|
|PF3D7_1323500||PEXEL protease plasmepsin V|