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A conserved domain of herpes simplex virus ICP34.5 regulates protein phosphatase complex in mammalian cells
Author(s) -
Zhang Cuizhu,
Tang Jun,
Xie Jia,
Zhang Hongkai,
Li Yapeng,
Zhang Jie,
Verpooten Dustin,
He Bin,
Cao Youjia
Publication year - 2008
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2007.11.082
Subject(s) - dephosphorylation , protein phosphatase 1 , herpes simplex virus , protein subunit , phosphatase , microbiology and biotechnology , biology , phosphorylation , viral tegument , sh3 domain , effector , virology , virus , biochemistry , proto oncogene tyrosine protein kinase src , gene
ICP34.5, encoded by herpes simplex virus 1, is a protein phosphatase 1 (PP1) regulatory subunit that mediates dephosphorylation of the α subunit of translation initiation factor 2 (eIF2α). 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 eIF2α dephosphorylation and viral protein synthesis.