Heterologous Expression, Purification, and Functional Analysis of Plasmodium falciparum Phosphatidylinositol 3′-Kinase

Biochemistry ◽  
2017 ◽  
Vol 56 (33) ◽  
pp. 4335-4345 ◽  
Author(s):  
Matthew R. Hassett ◽  
Anna R. Sternberg ◽  
Bryce E. Riegel ◽  
Craig J. Thomas ◽  
Paul D. Roepe
Keyword(s):  
Functional Analysis ◽  
Plasmodium Falciparum ◽  
Heterologous Expression ◽  
Phosphatidylinositol 3 Kinase ◽  
Phosphatidylinositol 3

scholarly journals In vivo Functional Analysis of the Counterbalance of Hyperactive Phosphatidylinositol 3-Kinase p110 Catalytic Oncoproteins by the Tumor Suppressor PTEN

2007 ◽  
Vol 67 (20) ◽  
pp. 9731-9739 ◽  
Author(s):  
Amparo Andrés-Pons ◽  
Isabel Rodríguez-Escudero ◽  
Anabel Gil ◽  
Ana Blanco ◽  
Ana Vega ◽  
...  
Keyword(s):  
Functional Analysis ◽  
Tumor Suppressor ◽  
Phosphatidylinositol 3 Kinase ◽  
Phosphatidylinositol 3

scholarly journals PfPI3K, a phosphatidylinositol-3 kinase from Plasmodium falciparum, is exported to the host erythrocyte and is involved in hemoglobin trafficking

Blood ◽  
2010 ◽  
Vol 115 (12) ◽  
pp. 2500-2507 ◽  
Author(s):  
Ankush Vaid ◽  
Ravikant Ranjan ◽  
Wynand A. Smythe ◽  
Heinrich C. Hoppe ◽  
Pushkar Sharma
Keyword(s):  
Plasmodium Falciparum ◽  
Malaria Parasite ◽  
Second Messengers ◽  
Active Form ◽  
Food Vacuole ◽  
Parasite Growth ◽  
Phosphatidylinositol 3 Kinase ◽  
Pi3k Inhibitors ◽  
Parasite Plasmodium ◽  
Phosphatidylinositol 3

Abstract Polyphosphorylated phosphoinositides (PIPs) are potent second messengers, which trigger a wide variety of signaling and trafficking events in most eukaryotic cells. However, the role and metabolism of PIPs in malaria parasite Plasmodium have remained largely unexplored. Our present studies suggest that PfPI3K, a novel phosphatidylinositol-3-kinase (PI3K) in Plasmodium falciparum, is exported to the host erythrocyte by the parasite in an active form. PfPI3K is a versatile enzyme as it can generate various 3′-phosphorylated PIPs. In the parasite, PfPI3K was localized in vesicular compartments near the membrane and in its food vacuole. PI3K inhibitors wortmannin and LY294002 were effective against PfPI3K and were used to study PfPI3K function. We found that PfPI3K is involved in endocytosis from the host and trafficking of hemoglobin in the parasite. The inhibition of PfPI3K resulted in entrapment of hemoglobin in vesicles in the parasite cytoplasm, which prevented its transport to the food vacuole, the site of hemoglobin catabolism. As a result, hemoglobin digestion, which is a source of amino acids necessary for parasite growth, was attenuated and caused the inhibition of parasite growth.

Possibility of distinct insulin-signaling pathways beyond phosphatidylinositol 3-kinase-mediating glucose transport and lipogenesis

Diabetes ◽  
1998 ◽  
Vol 47 (2) ◽  
pp. 179-185 ◽  
Author(s):  
R. W. Stevenson ◽  
D. K. Kreutter ◽  
K. M. Andrews ◽  
P. E. Genereux ◽  
E. M. Gibbs
Keyword(s):  
Signaling Pathways ◽  
Glucose Transport ◽  
Insulin Signaling ◽  
Phosphatidylinositol 3 Kinase ◽  
Phosphatidylinositol 3
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