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Several proteins which specifically bind to PKC have been classified as RACKs (receptors for activated C-kinase). RACK1 was cloned from a rat brain cDNA expression library by screening for proteins that bind PKC in the presence of phosphatidylserine, diacylglycerol, and calcium in a PKC overlay assay. By sequence homology, RACK1 appears to belong to a superfamily that includes the β subunit of G proteins. All of these proteins contain five to eight internal repeat elements known as WD40 motifs, which appear to have a role in protein-protein interactions. In addition, RACK1 contains two short sequences homologous to a PKC-binding sequence identified in Annexin I and in the brain PKC inhibitor KCIP. The binding of RACK1 to PKC is dose-dependent and occurs at a site on PKC that is distinct from the catalytic domain, indicating that RACK1 is not a PKC substrate.Immunofluorescence, Immunohistochemistry, Immunoprecipitation, Western Blotting
