Cytoskeleton (Hoboken). 2012 Oct 1. doi: 10.1002/cm.21077. [Epub ahead of print]
Targeted proteomic dissection of Toxoplasma cytoskeleton sub-compartments using MORN
Lorestani A, Ivey FD, Thirugnanam S, Busby MA, Marth GT, Cheeseman IM, Gubbels MJ.
Boston College, Department of Biology, Chestnut Hill, MA 02467, USA.
The basal complex in Toxoplasma functions as the contractile ring in the cell division process. Basal complex contraction tapers the daughter cytoskeleton toward the basal end and is required for daughter segregation. We have previously shown that the protein MORN1 is essential for basal complex assembly and likely acts as a scaffolding protein. To further our understanding of the basal complex we combined subcellular fractionation with an affinity purification of the MORN1 complex and identified its protein composition. We identified two new components of the basal complex, one of which uniquely associated with the basal complexin mature parasites, the first of its kind. In addition, we identified several other novel cytoskeleton proteins with different spatiotemporal dynamics throughout cell division. Since many of these proteins are unique to Apicomplexa this study significantly contributes to the annotation of their unique cytoskeleton. Furthermore we show that G-actin binding protein TgCAP is localized at the apical cap region in intracellular parasites, but quickly re-distributes to a cytoplasmic localization pattern upon egress. © 2012 Wiley-Blackwell, Inc.
PMID: 23027733 [PubMed - as supplied by publisher]