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Differential requirements for cyclase-associated protein (CAP) in actin-dependent processes of Toxoplasma gondii.


ABSTRACT: Toxoplasma gondii contains a limited subset of actin binding proteins. Here we show that the putative actin regulator cyclase-associated protein (CAP) is present in two different isoforms and its deletion leads to significant defects in some but not all actin dependent processes. We observe defects in cell-cell communication, daughter cell orientation and the juxtanuclear accumulation of actin, but only modest defects in synchronicity of division and no defect in the replication of the apicoplast. 3D electron microscopy reveals that loss of CAP results in a defect in formation of a normal central residual body, but parasites remain connected within the vacuole. This dissociates synchronicity of division and parasite rosetting and reveals that establishment and maintenance of the residual body may be more complex than previously thought. These results highlight the different spatial requirements for F-actin regulation in Toxoplasma which appear to be achieved by partially overlapping functions of actin regulators.

SUBMITTER: Hunt A 

PROVIDER: S-EPMC6785269 | biostudies-literature | 2019 Oct

REPOSITORIES: biostudies-literature

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Differential requirements for cyclase-associated protein (CAP) in actin-dependent processes of <i>Toxoplasma gondii</i>.

Hunt Alex A   Russell Matthew Robert Geoffrey MRG   Wagener Jeanette J   Kent Robyn R   Carmeille Romain R   Peddie Christopher J CJ   Collinson Lucy L   Heaslip Aoife A   Ward Gary E GE   Treeck Moritz M  

eLife 20191002


<i>Toxoplasma gondii</i> contains a limited subset of actin binding proteins. Here we show that the putative actin regulator cyclase-associated protein (CAP) is present in two different isoforms and its deletion leads to significant defects in some but not all actin dependent processes. We observe defects in cell-cell communication, daughter cell orientation and the juxtanuclear accumulation of actin, but only modest defects in synchronicity of division and no defect in the replication of the ap  ...[more]

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