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First published online 3 June 2008
doi: 10.1242/jcs.021154
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1 Bernhard Nocht Institute for Tropical Medicine, Malaria II, Bernhard-Nocht-Strasse 74, 20359 Hamburg, Germany
2 German Armed Forces, Bernhard Nocht Institute for Tropical Medicine, 20359 Hamburg, Germany
3 School of Biological Sciences, Nanyang Technological University, 637551, Singapore
4 Department of Immunology and Infectious Diseases, Harvard School of Public Health, Boston, MA, USA
5 The Walter and Eliza Hall Institute of Medical Research, Melbourne 3050, Australia
* Author for correspondence (e-mail: gilberger{at}bni-hamburg.de)
Accepted 17 April 2008
Summary
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.
Key words: Secretory pathway, Golgi, GRASP, Splice variant, Plasmodium
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