Export of malaria proteins requires co-translational processing of the PEXEL motif independent of phosphatidylinositol-3-phosphate binding

• DOI: 10.1038/ncomms10470
• Publication Date: 2016-02-01T09:47:58Z
• Authors: Justin A. Boddey; Matthew T. O’Neill; Sash Lopaticki; Teresa G. Carvalho; Anthony N. Hodder; Thomas Nebl; Stephan Wawra; Pieter van West; Zeinab Ebrahimzadeh; Dave Richard; Sven Flemming; Tobias Spielmann; Jude Przyborski; Jeff J. Babon; Alan F. Cowman
• Keywords: Nuclear export signal

Abstract Plasmodium falciparum exports proteins into erythrocytes using the export element (PEXEL) motif, which is cleaved in endoplasmic reticulum (ER) by plasmepsin V (PMV). A recent study reported that phosphatidylinositol-3-phosphate (PI(3)P) concentrated ER binds to PEXEL motifs and required for independent of PMV, are functionally interchangeable with RxLR oomycete effectors. Here we show does not bind PI(3)P, this lipid ER. We find cannot mediate P. . Parasites expressing a mutated version KAHRP, motif repositioned near signal sequence, prevented PMV cleavage. This mutant possessed putative PI(3)P-binding residues but exported. Reinstatement its original location restores processing export. These results challenge PI(3)P hypothesis provide evidence position conserved co-translational