Publications & Reports

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

Struck NS, Herrmann S, Langer C, Krueger A, Foth BJ, Engelberg K, Cabrera AL, Haase S, Treeck M, Marti M, Cowman AF, Spielmann T, Gilberger TW
Bernhard Nocht Institute for Tropical Medicine, Malaria II, Bernhard-Nocht-Strasse 74, 20359 Hamburg, Germany.

Abstract

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.

Publication

  • Journal: Journal of Cell Science
  • Published: 01/07/2008
  • Volume: 121
  • Issue: Pt 13
  • Pagination: 2123-2129

Author