| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1936972 | Biochemical and Biophysical Research Communications | 2007 | 7 Pages |
Receptor for activated C kinase 1 (RACK1) has been implicated in multiple protein–protein interactions including functioning as a scaffolding protein for signaling molecules. We report the cloning and cellular localization of a RACK1 ortholog (TgRACK1) in the opportunistic pathogen Toxoplasma gondii. The full-length transcript possesses a predicted ORF of 966 bp and codes for a protein of ∼35 kDa molecular weight. Molecular analysis of TgRACK1 reveals the presence of seven WD40 repeat motifs. TgRACK1 was tagged with a FLAG epitope and stably expressed in RH parasites. FLAG-TgRACK1 localizes to the parasite cytoplasm and nucleus. Immunoprecipitation (IP) of FLAG-TgRACK1 from highly purified extracellular parasites followed by immunoblot analysis reveals an interaction between TgβCOP and FLAG-TgRACK1. This is the first demonstration of an interaction between a βCOP subunit and the RACK1 protein. This result is of interest given that a signaling event precedes protein secretion and parasite invasion.
