Intracellular receptors for activated protein kinase C. Identification of a binding site for the enzyme - PubMed (original) (raw)
. 1991 Aug 15;266(23):14866-8.
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- PMID: 1831196
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Intracellular receptors for activated protein kinase C. Identification of a binding site for the enzyme
D Mochly-Rosen et al. J Biol Chem. 1991.
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Abstract
Protein kinase C (PKC) isozymes comprise a family of cytosolic enzymes that translocate to different intracellular sites on activation. We have recently characterized at least two intracellular receptor proteins for PKC (termed RACKs for receptors for activated C-kinase) in the Triton-insoluble material of the particulate fraction from neonatal rat heart. Here, we identify a sequence that appears to resemble the PKC binding site on these RACKs. A peptide (peptide I) with the sequence KGDYEKILVALCGGN bound PKC, and binding was markedly increased in the presence of PKC activators. Furthermore, peptide I inhibited PKC binding to RACKs in a dose-dependent manner. These data suggest that these RACKs have a common PKC binding sequence. Since peptide I inhibited PKC binding to RACKs in vitro, it may be a useful tool to inhibit PKC translocation and subsequent function in vivo.
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