dictyNews Electronic Edition Volume 40, number 15 June 20, 2014 Please submit abstracts of your papers as soon as they have been accepted for publication by by using the form at http://dictybase.org/db/cgi-bin/dictyBase/abstract_submit or by sending them to dicty@northwestern.edu Back issues of dictyNews, the Dicty Reference database and other useful information is available at dictyBase - http://dictybase.org. Follow dictyBase on twitter: http://twitter.com/dictybase ========= Abstracts ========= The Dictyostelium discoideum RACK1 orthologue has roles in growth and development Omosigho, N. N., Swaminathan, K., Plomann, M, Mźller-Taubenberger, A., Noegel, A. A., Riyahi, T. Y. Institute of Biochemistry I, Medical Faculty, Center for Molecular Medicine Cologne (CMMC) and Cologne Excellence Cluster on Cellular Stress Responses in Aging-Associated Diseases (CECAD), University of Cologne, 50931 Kšln, Germany Institute of Biochemistry II, Medical Faculty, University of Cologne, 50931 Kšln, Germany Institute of Anatomy and Cell Biology, Ludwig-Maximilians-University, 80336 Mźnchen, Germany Cell Commun Signal, in press 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, pulldown, 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. Submitted by Angelika Noegel [noegel@uni-koeln.de] ============================================================== [End dictyNews, volume 40, number 15]