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

Journal of Cell Science 121, 2123-2129 (2008)
Published by The Company of Biologists 2008
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Short Report

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

Nicole S. Struck1, Susann Herrmann1, Christine Langer1, Andreas Krueger2, Bernardo J. Foth3, Klemens Engelberg1, Ana L. Cabrera1, Silvia Haase1, Moritz Treeck1, Matthias Marti4, Alan F. Cowman5, Tobias Spielmann1 and Tim W. Gilberger1,*

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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