Article

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

College of Life Science, Nankai University, 94 Weijin Road, Tianjin 300071, PR China.
FEBS Letters (impact factor: 3.54). 02/2008; 582(2):171-6. DOI:10.1016/j.febslet.2007.11.082 pp.171-6
Source: PubMed

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.

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Keywords

alpha subunit
 
amino acid substitutions
 
arginine-rich motif
 
consensus PP1 binding motif
 
effector domain
 
eIF2alpha
 
eIF2alpha dephosphorylation
 
herpes simplex virus 1
 
phenotypes parallel
 
PP1 binding domain
 
protein phosphatase 1