Plasmodium falciparum possesses two GRASP proteins that are differentially targeted to the Golgi complex via a higher- and lower-eukaryote-like mechanism
- Struck, NS; Herrmann, S; Langer, C; Krueger, A; Foth, BJ; Engelberg, K; Cabrera, AL; Haase, S; Treeck, M; Marti, M; Cowman, AF; Spielmann, T; Gilberger, TW;
Publication Year 2008-07-01, Volume 121, Issue #13, Page 2123-2129
- Journal Title
- JOURNAL OF CELL SCIENCE
- Publication Type
- Journal Article
- 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.
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- MALARIA PARASITES; SEQUENCE ALIGNMENT; STACKING FACTOR; LOCALIZATION; IDENTIFICATION; TRANSFECTION; CISTERNAE; SEPARATION; PEPTIDES; CLEAVAGE
- Publisher's Version
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Creation Date: 2008-07-01 12:00:00Last Modified: 0001-01-01 12:00:00