The βγ Subunit of Heterotrimeric G Proteins Interacts with RACK1 and Two Other WD Repeat Proteins*
By Edward J. Dell, Jennifer Connor, Songhai Chen, E. Stebbins, N. Skiba, D. Mochly‐Rosen, Heidi E. Hamm. Journal of Biological Chemistry, 2002
91 citations recorded by the source corpus.
A yeast two-hybrid approach was used to discern possible new effectors for the βγ subunit of heterotrimeric G proteins. Three of the clones isolated are structurally similar to Gβ, each exhibiting the WD40 repeat motif. Two of these proteins, thereceptor for activated C kinase 1 (RACK1) and the dynein intermediate chain, co-immunoprecipitate with Gβγ using an anti-Gβ antibody. The third protein, AAH20044, has no known function; however, sequence analysis indicates that it is a WD40 repeat protein. Further investigation with RACK1 shows that it not only interacts with Gβ1γ1 but also unexpectedly with the transducin heterotrimer Gαtβ1γ1. Gαtalone does not interact, but it must contribute to the interaction because the apparent EC50 value of RACK1 for Gαtβ1γ1 is 3-fold greater than that for Gβ1γ1 (0.1 versus0.3 μm). RACK1 is a scaffold that interacts with several proteins, among which are activated βIIPKC and dynamin-1 (1). βIIPKC and dynamin-1 compete with Gβ1γ1and Gαtβ1γ1 for interaction with RACK1. These findings have several implications: 1) that WD40 repeat proteins may interact with each other; 2) that Gβγ interacts differently with RACK1 than with its other known effectors; and/or 3) that the G protein-RACK1 complex may constitute a signaling scaffold important for intracellular responses.
Subfields: Cell Biology, Molecular Biology
View Paper: https://www.semanticscholar.org/paper/954cecec1e882cdce11b59f1469a45f673a1b876
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Citations in the corpus
- Insights into G protein structure, function, and regulation. (2003, background): “Recently, our laboratory found that the receptor for activated C kinase 1 and the dynein intermediate chain interact with the G 1 1-dimer (131).”
- RACK1, A multifaceted scaffolding protein: Structure and function (2011, unknown): “RACK1 also forms a heterodimer with at least one other WD-repeat protein, Gb [27,28,53].”