Inner membrane complex proteomics reveals a palmitoylation regulation critical for intraerythrocytic development of malaria parasite
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 f...
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| Format: | Article |
| Language: | English |
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eLife Sciences Publications Ltd
2022-07-01
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| Series: | eLife |
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| Online Access: | https://elifesciences.org/articles/77447 |
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| author | Pengge Qian Xu Wang Chuan-Qi Zhong Jiaxu Wang Mengya Cai Wang Nguitragool Jian Li Huiting Cui Jing Yuan |
| author_facet | Pengge Qian Xu Wang Chuan-Qi Zhong Jiaxu Wang Mengya Cai Wang Nguitragool Jian Li Huiting Cui Jing Yuan |
| author_sort | Pengge Qian |
| collection | DOAJ |
| description | 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, the complete repertoire of IMC proteins and their localization determinants remain unclear. Here we used biotin ligase (TurboID)-based proximity labeling to compile the proteome of the schizont IMC of the 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 the IMC localization of proteins during the schizont development. |
| first_indexed | 2024-04-12T16:51:29Z |
| format | Article |
| id | doaj.art-0d6273c4949d4f92a40bbdcc0f606640 |
| institution | Directory Open Access Journal |
| issn | 2050-084X |
| language | English |
| last_indexed | 2024-04-12T16:51:29Z |
| publishDate | 2022-07-01 |
| publisher | eLife Sciences Publications Ltd |
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| series | eLife |
| spelling | doaj.art-0d6273c4949d4f92a40bbdcc0f6066402022-12-22T03:24:23ZengeLife Sciences Publications LtdeLife2050-084X2022-07-011110.7554/eLife.77447Inner membrane complex proteomics reveals a palmitoylation regulation critical for intraerythrocytic development of malaria parasitePengge Qian0Xu Wang1Chuan-Qi Zhong2Jiaxu Wang3Mengya Cai4Wang Nguitragool5Jian Li6https://orcid.org/0000-0002-6397-2785Huiting Cui7Jing Yuan8https://orcid.org/0000-0002-8907-9143State Key Laboratory of Cellular Stress Biology, School of Life Sciences, Faculty of Medicine and Life Sciences, Xiamen University, Xiamen, ChinaState Key Laboratory of Cellular Stress Biology, School of Life Sciences, Faculty of Medicine and Life Sciences, Xiamen University, Xiamen, ChinaState Key Laboratory of Cellular Stress Biology, School of Life Sciences, Faculty of Medicine and Life Sciences, Xiamen University, Xiamen, ChinaXiamen Center for Disease Control and Prevention, Xiamen, ChinaState Key Laboratory of Cellular Stress Biology, School of Life Sciences, Faculty of Medicine and Life Sciences, Xiamen University, Xiamen, ChinaDepartment of Molecular Tropical Medicine and Genetics, Faculty of Tropical Medicine, Mahidol University, Ratchathewi, ThailandState Key Laboratory of Cellular Stress Biology, School of Life Sciences, Faculty of Medicine and Life Sciences, Xiamen University, Xiamen, ChinaState Key Laboratory of Cellular Stress Biology, School of Life Sciences, Faculty of Medicine and Life Sciences, Xiamen University, Xiamen, ChinaState Key Laboratory of Cellular Stress Biology, School of Life Sciences, Faculty of Medicine and Life Sciences, Xiamen University, Xiamen, ChinaMalaria 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, the complete repertoire of IMC proteins and their localization determinants remain unclear. Here we used biotin ligase (TurboID)-based proximity labeling to compile the proteome of the schizont IMC of the 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 the IMC localization of proteins during the schizont development.https://elifesciences.org/articles/77447malaria parasiteplasmodium yoeliiintraerythrocytic developmentinner membrane complexproteomicpalmitoylation |
| spellingShingle | Pengge Qian Xu Wang Chuan-Qi Zhong Jiaxu Wang Mengya Cai Wang Nguitragool Jian Li Huiting Cui Jing Yuan Inner membrane complex proteomics reveals a palmitoylation regulation critical for intraerythrocytic development of malaria parasite eLife malaria parasite plasmodium yoelii intraerythrocytic development inner membrane complex proteomic palmitoylation |
| title | Inner membrane complex proteomics reveals a palmitoylation regulation critical for intraerythrocytic development of malaria parasite |
| title_full | Inner membrane complex proteomics reveals a palmitoylation regulation critical for intraerythrocytic development of malaria parasite |
| title_fullStr | Inner membrane complex proteomics reveals a palmitoylation regulation critical for intraerythrocytic development of malaria parasite |
| title_full_unstemmed | Inner membrane complex proteomics reveals a palmitoylation regulation critical for intraerythrocytic development of malaria parasite |
| title_short | Inner membrane complex proteomics reveals a palmitoylation regulation critical for intraerythrocytic development of malaria parasite |
| title_sort | inner membrane complex proteomics reveals a palmitoylation regulation critical for intraerythrocytic development of malaria parasite |
| topic | malaria parasite plasmodium yoelii intraerythrocytic development inner membrane complex proteomic palmitoylation |
| url | https://elifesciences.org/articles/77447 |
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