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  • Title: High phosphorylation of HBV core protein by two alpha-type CK2-activated cAMP-dependent protein kinases in vitro.
    Author: Enomoto M, Sawano Y, Kosuge S, Yamano Y, Kuroki K, Ohtsuki K.
    Journal: FEBS Lett; 2006 Feb 06; 580(3):894-9. PubMed ID: 16430890.
    Abstract:
    Two alpha-type CK2-activated PKAs (CK2-aPKAIalpha and CK2-aPKAIIalpha) were biochemically characterized in vitro using GST-HBV core fusion protein (GST-Hcore) and GST-Hcore157B as phosphate acceptors. It was found that (i), in the absence of cAMP, these two CK2-aPKAs phosphorylated both Ser-170 and Ser-178 on GST-Hcore and Hcore157B; (ii) this phosphorylation was approx. 4-fold higher than their phosphorylation by cAMP-activated PKAs; and (iii) suramin effectively inhibited the phosphorylation of Hcore157B by CK2-aPKAIIalpha through its direct binding to Hcore157B in vitro. These results suggest that high phosphorylation of HBV-CP by two CK2-aPKAs, in the absence of cAMP, may be involved in the pregenomic RNA (pgRNA) encapsidation and DNA-replication in HBV-infected cells.
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