Abstract
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.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callMore From: Biochemical and Biophysical Research Communications
Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
