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First published online 3 June 2008
doi: 10.1242/jcs.021154

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Plasmodium falciparum possesses two GRASP proteins that are differentially targeted to the Golgi complex via a higher- and lower-eukaryote-like mechanism

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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