PI4-kinase and PfCDPK7 signaling regulate phospholipid biosynthesis in P. falciparum

ABSTRACT: PfCDPK7 is an atypical member of the Calcium-Dependent Protein Kinase (CDPK) family and is crucial for the development of Plasmodium falciparum. However, the mechanisms whereby PfCDPK7 regulates parasite development remain unknown. Here, we perform quantitative phosphoproteomics and phospholipid analysis and find that PfCDPK7 promotes phosphatidylcholine (PC) synthesis by regulating two key enzymes involved in PC synthesis, phosphoethanolamine-N-methyltransferase (PMT) and ethanolamine kinase (EK). In the absence of PfCDPK7 both enzymes are hyperphosphorylated and PMT is degraded. We further find that PfCDPK7 interacts with 4'-phosphorylated phosphoinositides (PIPs) generated by PI4-kinase. Inhibition of PI4K activity disrupts the vesicular localization PfCDPK7. P. falciparum PI4-kinase, P

SUBMITTER: Dr. Ranjana Maurya 

PROVIDER: S-SCDT-EMBOR-2021-54022-T | biostudies-other |

REPOSITORIES: biostudies-other