{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,29]],"date-time":"2026-09-29T20:31:28Z","timestamp":1790713888992,"version":"4.1.0"},"reference-count":43,"publisher":"American Society for Microbiology","issue":"5","license":[{"start":{"date-parts":[[2017,10,31]],"date-time":"2017-10-31T00:00:00Z","timestamp":1509408000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"},{"start":{"date-parts":[[2017,11,8]],"date-time":"2017-11-08T00:00:00Z","timestamp":1510099200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"funder":[{"DOI":"10.13039\/501100001407","name":"Department of Biotechnology , Ministry of Science and Technology","doi-asserted-by":"publisher","award":["BT\/COE\/34\/SP15138\/2015"],"award-info":[{"award-number":["BT\/COE\/34\/SP15138\/2015"]}],"id":[{"id":"10.13039\/501100001407","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["mBio"],"published-print":{"date-parts":[[2017,11,8]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n                  <jats:p>\n                    Mechanisms by which 3\u2032-phosphorylated phosphoinositides (3\u2032-PIPs) regulate the development of apicomplexan parasites\n                    <jats:italic>Plasmodium falciparum<\/jats:italic>\n                    and\n                    <jats:italic>Toxoplasma gondii<\/jats:italic>\n                    are poorly understood. The catabolic process of autophagy, which is dependent on autophagy-related proteins (ATGs), is one of the major targets of 3\u2032-PIPs in yeast and mammals. In the present study, we identified autophagy-related protein ATG18 as an effector of 3\u2032-PIPs in these parasites.\n                    <jats:italic>P<\/jats:italic>\n                    .\n                    <jats:italic>falciparum<\/jats:italic>\n                    ATG18 (PfATG18) and\n                    <jats:italic>T<\/jats:italic>\n                    .\n                    <jats:italic>gondii<\/jats:italic>\n                    ATG18 (TgATG18) interact with 3\u2032-PIPs but exhibited differences in their specificity of interaction with the ligand PIP. The conditional knockdown of\n                    <jats:italic>T<\/jats:italic>\n                    .\n                    <jats:italic>gondii<\/jats:italic>\n                    or\n                    <jats:italic>P<\/jats:italic>\n                    .\n                    <jats:italic>falciparum<\/jats:italic>\n                    ATG18 (Tg\/PfATG18) impaired replication of parasites and resulted in their delayed death. Intriguingly, ATG18 depletion resulted in the loss of the apicomplexan parasite-specific nonphotosynthetic plastid-like organelle apicoplast, which harbors the machinery for biosynthesis of key metabolites, and the interaction of ATG18 to phosphatidylinositol 3-phosphate (PI3P) was critical for apicoplast inheritance. Furthermore, ATG18 regulates membrane association and apicoplast localization of ATG8. These findings provide insights into a novel noncanonical role of ATG18 in apicoplast inheritance. This function of ATG18 in organelle biogenesis is unprecedented in any organism and may be conserved across most apicomplexan parasites.\n                  <\/jats:p>\n                  <jats:p>\n                    <jats:bold>IMPORTANCE<\/jats:bold>\n                    Typically, autophagy is a catabolic process utilized by cells for their survival upon encountering nutrient-limiting conditions. The autophagy machinery is very tightly regulated, and autophagy-related genes (ATGs) play a pivotal role in this process. In the present study, we report a novel noncanonical function of autophagy-related protein ATG18 in inheritance of the nonphotosynthetic plastid-like organelle apicoplast in apicomplexan parasites\n                    <jats:italic>Plasmodium<\/jats:italic>\n                    and\n                    <jats:italic>Toxoplasma<\/jats:italic>\n                    . ATG18 depletion in these parasites resulted in \u201cdelayed death,\u201d which was the result of loss of apicoplast and impaired parasite division. Pf\/TgATG18 interact with 3\u2032-phosphorylated PIPs, which guide their cellular localization in the parasite, which is essential for their function.\n                  <\/jats:p>","DOI":"10.1128\/mbio.01468-17","type":"journal-article","created":{"date-parts":[[2017,10,31]],"date-time":"2017-10-31T20:10:14Z","timestamp":1509480614000},"update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":52,"title":["Autophagy-Related Protein ATG18 Regulates Apicoplast Biogenesis in Apicomplexan Parasites"],"prefix":"10.1128","volume":"8","author":[{"given":"Priyanka","family":"Bansal","sequence":"first","affiliation":[{"name":"Eukaryotic Gene Expression Laboratory, National Institute of Immunology, New Delhi, India"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Anuj","family":"Tripathi","sequence":"additional","affiliation":[{"name":"Eukaryotic Gene Expression Laboratory, National Institute of Immunology, New Delhi, 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