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Golgi architecture in the malaria parasite Plasmodium falciparum
Author(s) -
Gilberger TimWolf,
Herrmann Susann,
Treeck Moritz,
Cowman Alan,
Marti Matthias,
Struck Nicole Sunaina
Publication year - 2007
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.21.6.a1038-b
Subject(s) - golgi apparatus , plasmodium falciparum , biology , microbiology and biotechnology , secretory pathway , secretion , rab , secretory protein , brefeldin a , endoplasmic reticulum , malaria , gtpase , biochemistry , immunology
Plasmodium falciparum, the causative agent of malaria, relies on a sophisticated protein secretion system for host cell invasion and transformation. Although the parasite displays a secretory pathway similar to those of all eukaryotic organisms, it possesses a rather unique Golgi apparatus. In order to get a better understanding of Golgi morphology in Plasmodium we identified and characterized the Golgi matrix protein PfGRASP, a homologue of the Golgi re‐assembly stacking protein (GRASP) family. Our analysis revealed that although the genome of the parasite encodes only one grasp gene, two splice variants exist. This might be reminiscent of the two GRASP proteins present in other eukaryotic systems. Using GFP‐fusion proteins we visualized the subcellular distribution of the two PfGRASP proteins. To further dissect the spatial organization of the Golgi and its relationship with the ER we used the luminal ER marker protein BiP and the COPII marker protein Sec13p. We show that ER export competence lies within well‐defined specialized ER compartments adjacent to the Golgi apparatus.