| Literature DB >> 25573429 |
K M Kaderi Kibria1, Khushboo Rawat1, Christen M Klinger2, Gaurav Datta1, Manoj Panchal1, Shailja Singh1, Gayatri R Iyer1, Inderjeet Kaur1, Veena Sharma3, Joel B Dacks4, Asif Mohmmed5, Pawan Malhotra6.
Abstract
The human malaria parasite Plasmodium falciparum possesses sophisticated systems of protein secretion to modulate host cell invasion and remodeling. In the present study, we provide insights into the function of the AP-1 complex in P. falciparum. We utilized GFP fusion constructs for live cell imaging, as well as fixed parasites in immunofluorescence analysis, to study adaptor protein mu1 (Pfμ1) mediated protein trafficking in P. falciparum. In trophozoites Pfμ1 showed similar dynamic localization to that of several Golgi/ER markers, indicating Golgi/ER localization. Treatment of transgenic parasites with Brefeldin A altered the localization of Golgi-associated Pfμ1, supporting the localization studies. Co-localization studies showed considerable overlap of Pfμ1 with the resident rhoptry proteins, rhoptry associated protein 1 (RAP1) and Cytoadherence linked asexual gene 3.1 (Clag3.1) in schizont stage. Immunoprecipitation experiments with Pfμ1 and PfRAP1 revealed an interaction, which may be mediated through an intermediate transmembrane cargo receptor. A specific role for Pfμ1 in trafficking was suggested by treatment with AlF4, which resulted in a shift to a predominantly ER-associated compartment and consequent decrease in co-localization with the Golgi marker GRASP. Together, these results suggest a role for the AP-1 complex in rhoptry protein trafficking in P. falciparum.Entities:
Keywords: Adaptor protein complex-1 (AP-1); Clathrin; ER–Golgi network; Plasmodium falciparum; Trafficking; Vesicular trafficking
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Year: 2015 PMID： 25573429 DOI： 10.1016/j.bbamcr.2014.12.030
Source DB: PubMed Journal: Biochim Biophys Acta ISSN： 0006-3002