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A plastid two-pore channel essential for inter-organelle communication and growth of Toxoplasma gondii
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A plastid two-pore channel essential for inter-organelle communication and growth of Toxoplasma gondii
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Journal Article
A plastid two-pore channel essential for inter-organelle communication and growth of Toxoplasma gondii
2021
Overview
Two-pore channels (TPCs) are a ubiquitous family of cation channels that localize to acidic organelles in animals and plants to regulate numerous Ca
2+
-dependent events. Little is known about TPCs in unicellular organisms despite their ancient origins. Here, we characterize a TPC from
Toxoplasma gondii
, the causative agent of toxoplasmosis. TgTPC is a member of a novel clad of TPCs in Apicomplexa, distinct from previously identified TPCs and only present in coccidians. We show that TgTPC localizes not to acidic organelles but to the apicoplast, a non-photosynthetic plastid found in most apicomplexan parasites. Conditional silencing of TgTPC resulted in progressive loss of apicoplast integrity, severely affecting growth and the lytic cycle. Isolation of TPC
null
mutants revealed a selective role for TPCs in replication independent of apicoplast loss that required conserved residues within the pore-lining region. Using a genetically-encoded Ca
2+
indicator targeted to the apicoplast, we show that Ca
2+
signals deriving from the ER but not from the extracellular space are selectively transmitted to the lumen. Deletion of the
TgTPC gene
caused reduced apicoplast Ca
2+
uptake and membrane contact site formation between the apicoplast and the ER. Fundamental roles for TPCs in maintaining organelle integrity, inter-organelle communication and growth emerge.
Two-pore channels (TPCs) are cation channels that localize to acidic organelles to regulate Ca
2+
dependent events. Here, Li et al. characterize a TPC from
Toxoplasma gondii
(TgTPC) that localizes to the apicoplast, is critical for maintaining its integrity and relevant for Ca
2+
uptake from the ER through stabilizing inter-organelle contact.
Publisher
Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
Subject
/ 13/106
/ 13/31
/ 14/19
/ 14/28
/ 14/34
/ 14/35
/ 14/63
/ 147/143
/ 38/1
/ 45/23
/ 45/77
/ 96/34
/ 96/35
/ Calcium Channels - chemistry
/ Calcium Channels - metabolism
/ Cations
/ Cloning
/ Endoplasmic Reticulum - metabolism
/ Humanities and Social Sciences
/ Humans
/ Mutation
/ Proteins
/ Protozoan Proteins - chemistry
/ Protozoan Proteins - genetics
/ Protozoan Proteins - metabolism
/ Science
