ArticleCell communication and signaling : CCS2014
The Dictyostelium discoideum RACK1 orthologue has roles in growth and development.
Article in Cell communication and signaling : CCS, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 9 citations in OpenAlex.
- Related Dictyostelium G protein subunits Gα1 and Gα2 have different roles in chemotaxis and transcription factor regulation.BMC molecular and cell biology · 2025Article
- RACK1 evolved species-specific multifunctionality in translational control through sequence plasticity within a loop domain.Journal of cell science · 2019Article
- MoMip11, a MoRgs7-interacting protein, functions as a scaffolding protein to regulate cAMP signaling and pathogenicity in the rice blast fungus Magnaporthe oryzae.Environmental microbiology · 2018Article
- High expression of RACK1 is associated with poor prognosis in patients with pancreatic ductal adenocarcinoma.Oncology letters · 2018Article
- Article
- AealRACK1 expression and localization in response to stress in C6/36 HT mosquito cells.Journal of proteomics · 2015Article
- The Receptor for Activated C Kinase in Plant Signaling: Tale of a Promiscuous Little Molecule.Frontiers in plant science · 2015Review
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Authors and funding
6 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundThe receptor for activated C-kinase 1 (RACK1) is a conserved protein belonging to the WD40 repeat family of proteins. It folds into a beta propeller with seven blades which allow interactions with many proteins. Thus it can serve as a scaffolding protein and have roles in several cellular processes.
resultsWe identified the product of the Dictyostelium discoideum gpbB gene as the Dictyostelium RACK1 homolog. The protein is mainly cytosolic but can also associate with cellular membranes. DdRACK1 binds to phosphoinositides (PIPs) in protein-lipid overlay and liposome-binding assays. The basis of this activity resides in a basic region located in the extended loop between blades 6 and 7 as revealed by mutational analysis. Similar to RACK1 proteins from other organisms DdRACK1 interacts with G protein subunits alpha, beta and gamma as shown by yeast two-hybrid, pulldown, and immunoprecipitation assays. Unlike the Saccharomyces cerevisiae and Cryptococcus neoformans RACK1 proteins it does not appear to take over Gβ function in D. discoideum as developmental and other defects were not rescued in Gβ null mutants overexpressing GFP-DdRACK1. Overexpression of GFP-tagged DdRACK1 and a mutant version (DdRACK1mut) which carried a charge-reversal mutation in the basic region in wild type cells led to changes during growth and development.
conclusionDdRACK1 interacts with heterotrimeric G proteins and can through these interactions impact on processes specifically regulated by these proteins.
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