Abstract
One of protein kinase C (PKC) isozymes, PKC β binds to receptor for activated C kinase 1 (RACK1), and their complex is suggested to be translocated to melanosomes. The binding site of PKC β for RACK1 is considered one of its catalytic domains, V5 domain which consists of three motifs such as V5-1, V5-2, and V5-3. Among these, V5-1 region, extreme C-terminal residues of PKC β showed the highest RACK1-binding affinity. PKC β can be classified into PKC βI and PKC βII based on their different V5 domains. RACK1-binding affinity of PKC βII is five times greater than that of PKC βI. The structures of PKC βI, PKC βII, and RACK1 are not known. However, the conformational study on PKC βII V5-1 region showing high RACK1-binding selectivity may help us in understanding the interaction between RACK1 and PKC βII.
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