[HTML][HTML] C2 Region-derived Peptides Inhibit Translocation and Function of β Protein Kinase C in Vivo (∗)
D Ron, J Luo, D Mochly-Rosen - Journal of biological chemistry, 1995 - ASBMB
RACK1 is a protein kinase C (PKC)-binding protein that fulfills the criteria previously
established for a receptor for activated C-kinase (RACK). If binding of PKC to RACK anchors
the activated enzyme near its protein substrates, then inhibition of this binding should inhibit
translocation and function of the enzyme in vivo. Here, we have identified such inhibitors that
mimic the RACK1-binding site on βPKC. We first found that a C2-containing fragment, but
not a C1-containing fragment of βPKC, bound to RACK1 and inhibited subsequent βPKC …
established for a receptor for activated C-kinase (RACK). If binding of PKC to RACK anchors
the activated enzyme near its protein substrates, then inhibition of this binding should inhibit
translocation and function of the enzyme in vivo. Here, we have identified such inhibitors that
mimic the RACK1-binding site on βPKC. We first found that a C2-containing fragment, but
not a C1-containing fragment of βPKC, bound to RACK1 and inhibited subsequent βPKC …