Inner membrane complex proteomics reveals a palmitoylation regulation critical for intraerythrocytic development of malaria parasite
Issued Date
2022-07-01
Resource Type
eISSN
2050084X
Scopus ID
2-s2.0-85134632114
Pubmed ID
35775739
Journal Title
eLife
Volume
11
Rights Holder(s)
SCOPUS
Bibliographic Citation
eLife Vol.11 (2022)
Suggested Citation
Qian P. Inner membrane complex proteomics reveals a palmitoylation regulation critical for intraerythrocytic development of malaria parasite. eLife Vol.11 (2022). doi:10.7554/elife.77447 Retrieved from: https://repository.li.mahidol.ac.th/handle/20.500.14594/83681
Title
Inner membrane complex proteomics reveals a palmitoylation regulation critical for intraerythrocytic development of malaria parasite
Author(s)
Other Contributor(s)
Abstract
Malaria is caused by infection of the erythrocytes by the parasites Plasmodium. Inside the erythrocytes, the parasites multiply via schizogony, an unconventional cell division mode. The Inner Membrane Complex (IMC), an organelle located beneath the parasite plasma membrane, serving as the platform for protein anchorage, is essential for schizogony. So far, complete repertoire of IMC proteins and their localization determinants remain unclear. Here we used biotin ligase (TurboID)-based proximity labelling to compile the proteome of the schizont IMC of rodent malaria parasite Plasmodium yoelii. In total, 300 TurboID-interacting proteins were identified. 18 of 21 selected candidates were confirmed to localize in the IMC, indicating good reliability. In light of the existing palmitome of Plasmodium falciparum, 83 proteins of the P. yoelii IMC proteome are potentially palmitoylated. We further identified DHHC2 as the major resident palmitoyl-acyl-transferase of the IMC. Depletion of DHHC2 led to defective schizont segmentation and growth arrest both in vitro and in vivo. DHHC2 was found to palmitoylate two critical IMC proteins CDPK1 and GAP45 for their IMC localization. In summary, this study reports an inventory of new IMC proteins and demonstrates a central role of DHHC2 in governing IMC localization of proteins during the schizont development.