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An Apicomplexan Actin-Binding Protein Serves as a Connector and Lipid Sensor to Coordinate Motility and Invasion

Pires, Isa
Stock, Jessica
Hung, Yu-Fu
Han, Huijong
Tewari, Rita
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Published in Cell Host & Microbe. 2016, vol. 20, no. 6, p. 731-743
Abstract Apicomplexa exhibit a unique form of substrate-dependent gliding motility central for host cell invasion and parasite dissemination. Gliding is powered by rearward translocation of apically secreted transmembrane adhesins via their interaction with the parasite actomyosin system. We report a conserved armadillo and pleckstrin homology (PH) domain-containing protein, termed glideosome-associated connector (GAC), that mediates apicomplexan gliding motility, invasion, and egress by connecting the micronemal adhesins with the actomyosin system. TgGAC binds to and stabilizes filamentous actin and specifically associates with the transmembrane adhesin TgMIC2. GAC localizes to the apical pole in invasive stages of Toxoplasma gondii and Plasmodium berghei, and apical positioning of TgGAC depends on an apical lysine methyltransferase, TgAKMT. GAC PH domain also binds to phosphatidic acid, a lipid mediator associated with microneme exocytosis. Collectively, these findings indicate a central role for GAC in spatially and temporally coordinating gliding motility and invasion.
PMID: 27978434
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Article (Published version) (5.2 MB) - document accessible for UNIGE members only Limited access to UNIGE
Research group Biologie d'un parasite intracellulaire obligatoire (773)
Projects FNS: 310030B_166678
FNS: 310030_147118
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JACOT, Damien et al. An Apicomplexan Actin-Binding Protein Serves as a Connector and Lipid Sensor to Coordinate Motility and Invasion. In: Cell Host & Microbe, 2016, vol. 20, n° 6, p. 731-743. https://archive-ouverte.unige.ch/unige:91051

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Deposited on : 2017-01-13

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