The TSP motif in AP180 inhibits phospholipase D1 activity resulting in increased efficacy of anticancer drug via its direct binding to carboxyl terminal of phospholipase D1
作者： Ju Hwan Cho , Doo-Yi Oh , Hyoung-Ju Kim , Shin-Young Park , Hye-Jin Choi
DOI: 10.1016/J.CANLET.2011.01.005
关键词:
摘要: Phospholipase D (PLD) has two isoforms, PLD1 and PLD2. Both isoforms are possible candidates for the development of anticancer drugs, since PLDs in several cancer cells act as survival factors. The aim this study was to elucidate inhibitory mechanism by AP180 human cells. Transfection (hAP180) gene markedly inhibited phobol-12-myristate 13-acetate-induced PLD activity resulting exacerbation drug-induced cell death. Experiments using deletion mutants hAP180 showed that three amino acids (Thr312–Pro314) critical inhibition binding directly PLD1, and, these, Ser313 most important residue both inhibiting PLD1. However, relationship did not exist between In addition, C-terminal region is interaction with hAP180. These results indicated Thr312–Pro314 (especially a phosphorylation residue) can regulate hPLD1 through
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