A conserved domain of herpes simplex virus ICP34.5 regulates protein phosphatase complex in mammalian cells

作者：Zhang Cuizhu; Tang Jun; Xie Jia; Zhang Hongkai; Li Yapeng; Zhang Jie; Verpooten Dustin; He Bin; Cao Youjia^*

来源：FEBS Letters, 2008, 582(2): 171-176.

DOI：10.1016/j.febslet.2007.11.082

• ICP34.5
• PP1
• eIF2 alpha
• arginine rich motif

ICP34.5, encoded by herpes simplex virus 1, is a protein phosphatase I (PP1) regulatory subunit that mediates dephosphorylation of the a subunit of translation initiation factor 2 (eIF2 alpha). However, the mechanism of its action remains poorly understood. Here, we show that amino acid substitutions in the arginine-rich motif have differential effects on ICP34.5 activity. The phenotypes parallel with viral protein synthesis and cytopathic effects in virus infected cells. Besides the consensus PP1 binding motif, the Arg-motif appears to enhance the interaction between ICP34.5 and PP1. These results suggest that concerted action between the PP1 binding domain and the effector domain of ICP34.5 is crucial for eIF2 alpha dephosphorylation and viral protein synthesis.

• 出版日期2008-1
• 单位南开大学