Jan 31, 2025 · Regulation of PKC activities has also been shown to be exerted by a family of proteins called receptors for activated C kinase (RACK) which are a family of membrane-associated PKC anchoring proteins. RACK serve as molecular scaffolds that localize individual PKC to distinct membrane microdomains in close proximity to their allosteric activators ...

Oct 6, 2011 · In addition, the RACK1/PKC partnership was suggested to be intrinsically linked and PKCs have been shown to regulate RACK1 expression in cardiac myocytes . As well as stabilising PKC activity, RACK1 introduces activated PKC to …

Oct 17, 2001 · Here, we describe the role of adaptor proteins in determining the specific function of individual protein kinase C (PKC) isozymes. These isozyme-selective proteins were called collectively...

Sep 1, 1997 · Recent studies have clarified the key role played by the anchoring proteins in mediating subcellular PKC location, that is, in driving the enzyme to specific sites of action. The protein, receptor for activated C-kinase 1 (RACK1) is involved in …

May 1, 1991 · Binding of PKC to two of these proteins was concentration-dependent, saturable, and specific, suggesting that these binding proteins are receptors for activated C-kinase, termed here "RACKs." PKC binds to RACKs via a site on PKC distinct from the substrate binding site.

Protein scaffolds such as A-kinase anchoring proteins (AKAPs) and receptors for activated C-kinase (RACKs) organize PKCs, their substrates, and their modulators into subcellular complexes that coordinate signaling.

Jan 17, 1995 · We have previously identified receptors for activated C kinase (RACKs) as components of protein kinase C (PKC) signaling. RACK1, a recently cloned 36-kDa RACK, has short sequences of homology to PKC.

Mar 1, 2001 · Our data demonstrate that activation of PKC modulates the expression of RACK isotypes and PKC-RACK interactions in a PKCε activity- and dosage-dependent fashion.

C. PKC Interactions With RACK Proteins. Models of PKC activation have generally focused on the intramolecular interaction between the pseudosubstrate domain and the catalytic pocket; PKC mutations that disrupt this intramolecular interaction (such as a pseudosubstrate domain deletion or an alanine→glutamate phosphomimetic substitution in the ...

In summary, we have shown that β′-COP fulfills the criteria for a PKCε-selective RACK: it binds activated PKCε better than any other isozyme, and PKC binding is dose-dependent and saturable. β′-COP co-immunoprecipitates and colocalizes with …