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

• Published in: Journal of cell science Vol. 121; no. 13; pp. 2123 - 2129
• Main Authors: Struck, Nicole S, Herrmann, Susann, Langer, Christine, Krueger, Andreas, Foth, Bernardo J, Engelberg, Klemens, Cabrera, Ana L, Haase, Silvia, Treeck, Moritz, Marti, Matthias, Cowman, Alan F, Spielmann, Tobias, Gilberger, Tim W
• Format: Journal Article
• Language: English
• Published: England The Company of Biologists Limited 01.07.2008
• Subjects: Amino Acid Sequence; Animals; Eukaryotic Cells; Evolution, Molecular; Golgi Apparatus - metabolism; Membrane Proteins - genetics; Membrane Proteins - metabolism; Molecular Sequence Data; Plasmodium falciparum; Plasmodium falciparum - genetics; Plasmodium falciparum - metabolism; Plasmodium falciparum - ultrastructure; Protein Transport - genetics; Protozoan Proteins - metabolism
• ISSN: 0021-9533; 1477-9137
• DOI: 10.1242/jcs.021154

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.