Dematin, a Component of the Erythrocyte Membrane Skeleton, Is Internalized by the Malaria Parasite and Associates with Plasmodium 14-3-3
Dematin, a Component of the Erythrocyte Membrane Skeleton, Is Internalized by the Malaria Parasite and Associates with Plasmodium 14-3-3
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DOI：
10.1074/jbc.m110.194613
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发表时间：
2011-01-14
影响因子：
4.8
通讯作者：
Ponzi, Marta
中科院分区：
文献类型：
--
作者：
Lalle, Marco;Curra, Chiara;Ponzi, Marta
疟疾寄生虫侵入终末分化的红细胞，并在寄生液泡包围下生长和繁殖。疟原虫血液阶段将新合成的蛋白质转移到寄生液泡外，并将它们引导至各种红细胞区室，包括细胞骨架和质膜。在这里，我们表明寄生虫指导的宿主细胞的重塑还包括脱蛋白（红细胞膜骨架的肌动蛋白结合蛋白）的募集及其对寄生虫的重新定位。内化脱蛋白被发现与疟原虫 14-3-3 相关，疟原虫属于保守的多任务分子家族。我们还表明，在体外，脱蛋白-14-3-3 相互作用严格依赖于脱蛋白 Ser(124) 和 Ser(333) 的磷酸化，属于两个 14-3-3 假定的结合基序。这项研究是第一份报告，表明红细胞感染后疟原虫会招募基于红细胞血影蛋白的膜骨架的一个成分。
The malaria parasite invades the terminally differentiated erythrocytes, where it grows and multiplies surrounded by a parasitophorous vacuole. Plasmodium blood stages translocate newly synthesized proteins outside the parasitophorous vacuole and direct them to various erythrocyte compartments, including the cytoskeleton and the plasma membrane. Here, we show that the remodeling of the host cell directed by the parasite also includes the recruitment of dematin, an actin-binding protein of the erythrocyte membrane skeleton and its repositioning to the parasite. Internalized dematin was found associated with Plasmodium 14-3-3, which belongs to a family of conserved multitask molecules. We also show that, in vitro, the dematin-14-3-3 interaction is strictly dependent on phosphorylation of dematin at Ser(124) and Ser(333), belonging to two 14-3-3 putative binding motifs. This study is the first report showing that a component of the erythrocyte spectrin-based membrane skeleton is recruited by the malaria parasite following erythrocyte infection.