Autophagy-related Atg8 localizes to the apicoplast of the human malaria parasite Plasmodium falciparum.

Autophagy-related Atg8 localizes to the apicoplast of the human malaria parasite Plasmodium falciparum.
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DOI:
10.1371/journal.pone.0042977
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发表时间:
2012
期刊:
影响因子:
3.7
通讯作者:
Mizushima N
Mizushima N
中科院分区:
综合性期刊3区
文献类型:
--
作者:
Kitamura K;Kishi-Itakura C;Tsuboi T;Sato S;Kita K;Ohta N;Mizushima N

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Autophagy is a membrane-mediated degradation process, which is governed by sequential functions of Atg proteins. Although Atg proteins are highly conserved in eukaryotes, protozoa possess only a partial set of Atg proteins. Nonetheless, almost all protozoa have the complete factors belonging to the Atg8 conjugation system, namely, Atg3, Atg4, Atg7, and Atg8. Here, we report the biochemical properties and subcellular localization of the Atg8 protein of the human malaria parasite Plasmodium falciparum (PfAtg8). PfAtg8 is expressed during intra-erythrocytic development and associates with membranes likely as a lipid-conjugated form. Fluorescence microscopy and immunoelectron microscopy show that PfAtg8 localizes to the apicoplast, a four membrane-bound non-photosynthetic plastid. Autophagosome-like structures are not observed in the erythrocytic stages. These data suggest that, although Plasmodium parasites have lost most Atg proteins during evolution, they use the Atg8 conjugation system for the unique organelle, the apicoplast.
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