Work

Intracellular receptors for activated protein kinase C. Identification of a binding site for the enzyme

Year: 1991

Type: article

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.

Source: Journal of Biological Chemistry

DOI: 10.1016/s0021-9258(18)98554-6

Authors: D. Mochly-Rosen, H. Khaner, J. Lopez, B.L. Smith

Institutions: San Francisco General Hospital, University of California, San Francisco, University of California San Francisco Medical Center

Language: English

Topic: Protein Kinase Regulation and GTPase Signaling

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: hybrid

Estimated APC paid: $3,430

OpenAlex ID: W1495423595

FWCI: 5.006

Cites: 27

Cited by: 207

Related to: 9