| Literature DB >> 18068675 |
Cuizhu Zhang1, Jun Tang, Jia Xie, Hongkai Zhang, Yapeng Li, Jie Zhang, Dustin Verpooten, Bin He, Youjia Cao.
Abstract
ICP34.5, encoded by herpes simplex virus 1, is a protein phosphatase 1 (PP1) regulatory subunit that mediates dephosphorylation of the alpha subunit of translation initiation factor 2 (eIF2alpha). 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 eIF2alpha dephosphorylation and viral protein synthesis.Entities:
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Year: 2007 PMID： 18068675 DOI： 10.1016/j.febslet.2007.11.082
Source DB: PubMed Journal: FEBS Lett ISSN： 0014-5793 Impact factor: 4.124