Open AccessRole of Protein Kinase C δ in Reactivation of Kaposi's Sarcoma-Associated Herpesvirus
Author(s) -
Einat Deutsch,
Adina Cohen,
Gila Kazimirsky,
Sara Dovrat,
Hadara Rubinfeld,
Chaya Brodie,
Ronit Sarid
Publication year - 2004
Publication title -
journal of virology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.617
H-Index - 292
eISSN - 1070-6321
pISSN - 0022-538X
DOI - 10.1128/jvi.78.18.10187-10192.2004
Subject(s) - rottlerin , protein kinase c , biology , lytic cycle , activator (genetics) , kaposi's sarcoma associated herpesvirus , gene isoform , virology , 12 o tetradecanoylphorbol 13 acetate , mutant , tetradecanoylphorbol acetate , microbiology and biotechnology , autophosphorylation , kinase , virus , cancer research , protein kinase a , herpesviridae , biochemistry , gene , viral disease , phorbol ester
TPA (12-O-tetradecanoylphorbol-13-acetate), a well-known activator of protein kinase C (PKC), can experimentally induce reactivation of Kaposi's sarcoma-associated herpesvirus (KSHV) in certain latently infected cells. We selectively blocked the activity of PKC isoforms by using GF 109203X or rottlerin and demonstrated that this inhibition largely decreased lytic KSHV reactivation by TPA. Translocation of the PKCdelta isoform was evident shortly after TPA stimulation. Overexpression of the dominant-negative PKCdelta mutant supported an essential role for the PKCdelta isoform in virus reactivation, yet overexpression of PKCdelta alone was not sufficient to induce lytic reactivation of KSHV, suggesting that additional signaling molecules participate in this pathway.