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First published online November 23, 2005
doi: 10.1242/10.1242/jcs.02673


Journal of Cell Science 118, 5603-5613 (2005)
Published by The Company of Biologists 2005
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Research Article

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

Nicole S. Struck1, Suzana de Souza Dias1, Christine Langer1, Matthias Marti2, J. Andrew Pearce2, Alan F. Cowman2 and Tim W. Gilberger1,*

1 Bernhard Nocht Institute for Tropical Medicine, Malaria II, Bernhard-Nocht-Str. 74, 20359 Hamburg, Germany
2 The Walter and Eliza Hall Institute of Medical Research, 1G Royal Parade, Melbourne 3050, Australia

* Author for correspondence (e-mail: gilberger{at}bni-hamburg.de)

Accepted 2 September 2005

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.

Key words: Golgi, GRASP, Plasmodium, Secretory pathway, Transfection




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