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

• DOI: 10.1242/jcs.021154
• Publication Date: 2008-06-04T02:39:14Z
• Authors: Nicole S. Struck; Susann Herrmann; Christine Langer; Andreas Krueger; Bernardo J. Foth; Klemens Engelberg; Ana L. Cabrera; Silvia Haase; Moritz Treeck; Matthias Marti; Alan F. Cowman; Tobias Spielmann; Tim W. Gilberger
• Keywords: Transport protein; Eukaryote; Protein Sorting Signals

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