Targeted proteomic dissection of Toxoplasma cytoskeleton sub-compartments using MORN1
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Author(s) • • • • • •
Lorestani, Alexander
Ivey, F. Douglas
Thirugnanam, Sivasakthivel
Busby, Michele A.
Marth, Gabor T.
Gubbels, Marc-Jan
Cheeseman, Iain M
Date Issued
October 2012
Journal
Cytoskeleton
Publisher
Wiley Blackwell
Citation
Lorestani, Alexander, F. Douglas Ivey, Sivasakthivel Thirugnanam, Michele A. Busby, Gabor T. Marth, Iain M. Cheeseman, and Marc-Jan Gubbels. “Targeted proteomic dissection of Toxoplasma cytoskeleton sub-compartments using MORN1.” Cytoskeleton 69, no. 12 (December 11, 2012): 1069-1085.
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Author's final manuscript
Abstract
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 complex in 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 redistributes to a cytoplasmic localization pattern upon egress.
MIT Department
Massachusetts Institute of Technology. Department of Biology
Whitehead Institute for Biomedical Research
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Creative Commons Attribution-Noncommercial-Share Alike 3.0
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DOI of Published Version
https://doi.org/10.1002/cm.21077