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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

Struck, Nicole S., Herrmann, Susann, Langer, Christine, Krueger, Andreas, Foth, Bernardo, Engelberg, Klemens, Cabrera, Ana L., Haase, Silvia, Treeck, Moritz, Marti, Matthias, Cowman, Alan F., Spielmann, Tobias and Gilberger, Tim W. 2008, Plasmodium falciparum possesses two GRASP proteins that are differentially targeted to the Golgi complex via a higher- and lower-eukaryote-like mechanism, Journal of cell science, vol. 121, no. 13, pp. 2123-2129, doi: 10.1242/jcs.021154.

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Title Plasmodium falciparum possesses two GRASP proteins that are differentially targeted to the Golgi complex via a higher- and lower-eukaryote-like mechanism
Author(s) Struck, Nicole S.
Herrmann, Susann
Langer, Christine
Krueger, Andreas
Foth, Bernardo
Engelberg, Klemens
Cabrera, Ana L.
Haase, Silvia
Treeck, Moritz
Marti, Matthias
Cowman, Alan F.
Spielmann, Tobias
Gilberger, Tim W.
Journal name Journal of cell science
Volume number 121
Issue number 13
Start page 2123
End page 2129
Total pages 7
Publisher The Company of Biologists Ltd.
Place of publication Cambridge, England
Publication date 2008
ISSN 0021-9533
1477-9137
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.
Language eng
DOI 10.1242/jcs.021154
Field of Research 110803 Medical Parasitology
060106 Cellular Interactions (incl Adhesion, Matrix, Cell Wall)
HERDC Research category C1.1 Refereed article in a scholarly journal
Copyright notice ©2008, The Company of Biologists
Persistent URL http://hdl.handle.net/10536/DRO/DU:30025961

Document type: Journal Article
Collection: School of Medicine
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