Plasmodium falciparum possesses two GRASP proteins that are differentially targeted to the Golgi complex via a higher- and lower-eukaryote-like mechanism.

Abstract

Plasmodium falciparum, the causative agent of malaria, relies on a complex protein-secretion system for protein targeting into numerous subcellular destinations. Recently, a homologue of the Golgi re-assembly stacking protein (GRASP) was identified and used to characterise the Golgi organisation in this parasite. Here, we report on the presence of a splice variant that leads to the expression of a GRASP isoform. Although the first GRASP protein (GRASP1) relies on a well-conserved myristoylation motif, the variant (GRASP2) displays a different N-terminus, similar to GRASPs found in fungi. Phylogenetic analyses between GRASP proteins of numerous taxa point to an independent evolution of the unusual N-terminus that could reflect unique requirements for Golgi-dependent protein sorting and organelle biogenesis in P. falciparum. Golgi association of GRASP2 depends on the hydrophobic N-terminus that resembles a signal anchor, leading to a unique mode of Golgi targeting and membrane attachment.

DOI: 10.1242/jcs.021154

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Cite this paper

@article{Struck2008PlasmodiumFP, title={Plasmodium falciparum possesses two GRASP proteins that are differentially targeted to the Golgi complex via a higher- and lower-eukaryote-like mechanism.}, author={Nicole S. Struck and Susann Herrmann and Christine Langer and Andreas Krueger and Bernardo J Foth and Klemens Engelberg and Ana L Cabrera and Silvia Haase and Moritz Treeck and Matthias Marti and Alan F Cowman and Tobias Spielmann and Tim Wolf Gilberger}, journal={Journal of cell science}, year={2008}, volume={121 Pt 13}, pages={2123-9} }