Conference Agenda
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Daily Overview |
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CP11.1: Cells, Molecules & Genes 2 - 5 min talks Location: Lecture Theatre 1 Session Chair: Ellis Joch, Griffith University Session Chair: Wisam Dawood, Griffith University | |
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Investigating phospholipid transport by the essential Plasmodium falciparum protein PfCSC1 Australian National University, Australia PfCSC1 is a protein found in Plasmodium falciparum that belongs to a family of osmosensitive cation channels, some members of which have been found to double as scramblases (ATP-independent phospholipid transporters). Mutations in PfCSC1 or a putative rhomboid protease (PfROM8) are associated with resistance against specific compounds, termed PfROM8/PfCSC1-linked compounds (R/CLCs). To understand the mode of action of these compounds, the function of PfCSC1 must be understood. Previous research shows that PfCSC1 is an essential ion channel that can be activated by R/CLCs, with Na+ being one of its substrates. Here, I present evidence that PfCSC1 doubles as a scramblase, capable of phospholipid transport in the parasite plasma membrane. The internalisation of a fluorescent phospholipid analogue (NBD-PS) was measured in ATP-depleted parasites under several conditions. Knockdown of PfCSC1 did not have a significant effect on NBD-PS internalisation. However, upon exposure to hypotonic conditions or R/CLCs – both predicted to activate PfCSC1 – parasites expressing a normal level of PfCSC1 displayed a significant increase in NBD-PS internalisation, whereas the response of parasites in which PfCSC1 was knocked down was less pronounced. The data suggest that while PfCSC1 is capable of phospholipid scrambling, it is likely not always active under physiological conditions. | |