Regulation of Plasmodium falciparum glideosome associated protein 45 (PfGAP45) phosphorylation.

PloS One
Divya C ThomasPushkar Sharma

Abstract

The actomyosin motor complex of the glideosome provides the force needed by apicomplexan parasites such as Toxoplasma gondii (Tg) and Plasmodium falciparum (Pf) to invade their host cells and for gliding motility of their motile forms. Glideosome Associated Protein 45 (PfGAP45) is an essential component of the glideosome complex as it facilitates anchoring and effective functioning of the motor. Dissection of events that regulate PfGAP45 may provide insights into how the motor and the glideosome operate. We found that PfGAP45 is phosphorylated in response to Phospholipase C (PLC) and calcium signaling. It is phosphorylated by P. falciparum kinases Protein Kinase B (PfPKB) and Calcium Dependent Protein Kinase 1 (PfCDPK1), which are calcium dependent enzymes, at S89, S103 and S149. The Phospholipase C pathway influenced the phosphorylation of S103 and S149. The phosphorylation of PfGAP45 at these sites is differentially regulated during parasite development. The localization of PfGAP45 and its association may be independent of the phosphorylation of these sites. PfGAP45 regulation in response to calcium fits in well with the previously described role of calcium in host cell invasion by malaria parasite.

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Dec 14, 2012·Future Medicinal Chemistry·Isabelle S LucetChristian Doerig
Sep 7, 2012·International Journal of Medical Microbiology : IJMM·Damien Jacot, Dominique Soldati-Favre
Mar 13, 2014·Cellular Microbiology·Clare R Harding, Markus Meissner
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Dec 8, 2017·Scientific Reports·Krishan KumarDavid L Narum
Jul 7, 2017·Nature Communications·Sudhir KumarPushkar Sharma

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Methods Mentioned

BETA
glycosylation
immunoprecipitation
transgenic
transfection
PCR
ELISA
electrophoresis
immunuprecipitation
myristoylation
co-immunoprecipitation

Software Mentioned

Clustal
Image J
Adobe photoshop
Axiovision

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