Re-defining the Golgi complex in Plasmodium falciparum using the novel Golgi marker PfGRASP

Struck, NS; Dias, SD; Langer, C; Marti, M; Pearce, JA; Cowman, AF; Gilberger, TW

Author(s): Struck, NS; Dias, SD; Langer, C; Marti, M; Pearce, JA; Cowman, AF; Gilberger, TW;
Details: Publication Year 2005-12-01,Volume 118,Issue #23,Page 5603-5613
Journal Title: JOURNAL OF CELL SCIENCE
Publication Type: Journal Article
Abstract: Plasmodium falciparum, the causative agent of malaria, relies on a sophisticated protein secretion system for host cell invasion and transformation. Although the parasite displays a secretory pathway similar to those of all eukaryotic organisms, a classical Golgi apparatus has never been described. We identified and characterised the putative Golgi matrix protein PfGRASP, a homologue of the Golgi re-assembly stacking protein (GRASP) family. We show that PfGRASP is expressed as a 70 kDa protein throughout the asexual life cycle of the parasite. We generated PfGRASP-GFP-expressing transgenic parasites and showed that this protein is localised to a single, juxtanuclear compartment in ring-stage parasites. The PfGRASP compartment is distinct from the ER, restricted within the boundaries of the parasite and colocalises with the cis-Golgi marker ERD2. Correct subcellular localisation of this Golgi matrix protein depends on a cross-species conserved functional myristoylation motif and is insensitive to Brefeldin A. Taken together our results define the Golgi apparatus in Plasmodium and depict the morphological organisation of the organelle throughout the asexual life cycle of the parasite.
Publisher: COMPANY OF BIOLOGISTS LTD
Keywords: PARASITE TOXOPLASMA-GONDII; BREFELDIN-A; MALARIA PARASITE; SECRETORY PATHWAY; HOST ERYTHROCYTE; ENDOPLASMIC-RETICULUM; RETROGRADE TRANSPORT; MEMBRANE-PROTEINS; STACKING FACTOR; RAB GTPASES
Publisher's Version: https://doi.org/10.1242/jcs.02673
Terms of Use/Rights Notice: Refer to copyright notice on published article.

Creation Date: 2005-12-01 12:00:00