Omosigho, Napoleon Nosa, Swaminathan, Karthic ORCID: 0000-0002-0981-7549, Plomann, Markus, Mueller-Taubenberger, Annette, Noegel, Angelika A. and Riyahi, Tanja Y. (2014). The Dictyostelium discoideum RACK1 orthologue has roles in growth and development. Cell Commun. Signal., 12. LONDON: BMC. ISSN 1478-811X
Full text not available from this repository.Abstract
Background: The 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. Results: We 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, pull-down, and immunoprecipitation assays. Unlike the Saccharomyces cerevisiae and Cryptococcus neoformans RACK1 proteins it does not appear to take over G beta function in D. discoideum as developmental and other defects were not rescued in G beta 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. Conclusion: DdRACK1 interacts with heterotrimeric G proteins and can through these interactions impact on processes specifically regulated by these proteins.
Item Type: | Journal Article | ||||||||||||||||||||||||||||
Creators: |
|
||||||||||||||||||||||||||||
URN: | urn:nbn:de:hbz:38-435723 | ||||||||||||||||||||||||||||
DOI: | 10.1186/1478-811X-12-37 | ||||||||||||||||||||||||||||
Journal or Publication Title: | Cell Commun. Signal. | ||||||||||||||||||||||||||||
Volume: | 12 | ||||||||||||||||||||||||||||
Date: | 2014 | ||||||||||||||||||||||||||||
Publisher: | BMC | ||||||||||||||||||||||||||||
Place of Publication: | LONDON | ||||||||||||||||||||||||||||
ISSN: | 1478-811X | ||||||||||||||||||||||||||||
Language: | English | ||||||||||||||||||||||||||||
Faculty: | Unspecified | ||||||||||||||||||||||||||||
Divisions: | Unspecified | ||||||||||||||||||||||||||||
Subjects: | no entry | ||||||||||||||||||||||||||||
Uncontrolled Keywords: |
|
||||||||||||||||||||||||||||
URI: | http://kups.ub.uni-koeln.de/id/eprint/43572 |
Downloads
Downloads per month over past year
Altmetric
Export
Actions (login required)
View Item |