Binding Specificity for RACK1 Resides in the V5 Region of βII Protein Kinase C*
By E. Stebbins, D. Mochly‐Rosen. Journal of Biological Chemistry, 2001
167 citations recorded by the source corpus.
Identification of selective anchoring proteins responsible for specialized localization of specific signaling proteins has led to the identification of new inhibitors of signal transduction, inhibitors of anchoring protein-ligand interactions. RACK1, the firstreceptor for activated C kinase identified in our lab, is a selective anchoring protein for βII protein kinase C (βIIPKC). We previously found that at least part of the RACK1-binding site resides in the C2 domain of βIIPKC (Ron, D., Luo, J., and Mochly-Rosen, D. (1995) J. Biol. Chem.270, 24180–24187). Here we show that the V5 domain also contains part of the RACK1-binding site in βIIPKC. In neonatal rat cardiac myocytes, the βIIV5-3 peptide (amino acids 645–650 in βIIPKC) selectively inhibited phorbol 12-myristate 13-acetate (PMA)-induced translocation of βIIPKC and not βIPKC. In addition, the βIIV5-3 peptide inhibited cardiac myocyte hypertrophy in PMA-treated cells. Interestingly, βIV5-3 (646–651 in βIPKC), a selective translocation inhibitor of βIPKC, also inhibited PMA-induced cardiac myocyte hypertrophy, demonstrating that both βI- and βIIPKC are essential for this cardiac function. Therefore, the βIIV5 domain contains part of the RACK1-binding site in βIIPKC; a peptide corresponding to this site is a selective inhibitor of βIIPKC and, hence, enables the identification of βIIPKC-selective functions.
Subfields: Molecular Biology
View Paper: https://www.semanticscholar.org/paper/11026a4452d6427388f1f8b2c04deb53a5bb4e40
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Citations in the corpus
- Structural Basis of Protein Kinase C Isoform Function (2008, background): “The observation that PMA-dependent cardiomyocyte hypertrophy is inhibited by either the PKC I or the PKC II translocation inhibitor peptides suggests that both PKC isoforms contribute to cardiac growth responses (200).”
- RACK1, A multifaceted scaffolding protein: Structure and function (2011, unknown): “RACK1 binds activated PKCbII and the interaction serves to stabilize the active conformation of the kinase [42,45,60] (Figure 3).”