Plasmodium falciparum possesses two GRASP proteins that are differentially targeted to the Golgi complex via a higher- and lower-eukaryote-like mechanism
Details
Publication Year 2008-07-01, Volume 121, Issue #13, Page 2123-2129
Journal Title
JOURNAL OF CELL SCIENCE
Publication Type
Journal Article
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.
Publisher
COMPANY OF BIOLOGISTS LTD
Keywords
MALARIA PARASITES; SEQUENCE ALIGNMENT; STACKING FACTOR; LOCALIZATION; IDENTIFICATION; TRANSFECTION; CISTERNAE; SEPARATION; PEPTIDES; CLEAVAGE
Rights Notice
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Creation Date: 2008-07-01 12:00:00
Last Modified: 0001-01-01 12:00:00
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