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Intracellular receptors for activated protein kinase C. Identification of a binding site for the enzyme
Open accessAbstract
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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Metadata
- Authors
- Mochly-Rosen, D., Khaner, H., Lopez, J., & Smith, B. L.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1991-08
- Volume
- 266
- Issue
- 23
- Pages
- 14866-14868
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1495423595
- Cited by
- 211
- References
- 0
- FWCI
- 5.71
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Mochly-Rosen, D., Khaner, H., Lopez, J., & Smith, B. L. (1991). Intracellular receptors for activated protein kinase C. Identification of a binding site for the enzyme. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(18)98554-6
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