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A more recent version of this article appeared on May 31, 2002
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M111872200v1
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Papers In Press, published online ahead of print March 23, 2002
J. Biol. Chem, 10.1074/jbc.M111872200
Submitted on December 13, 2001
Revised on March 20, 2002
Accepted on March 22, 2002

Phosphorylation of varicella-zoster virus IE63 protein by casein kinases influences its cellular localization and gene regulation activity

Sebastien Bontems, Emmanuel Di Valentin, Laurence Baudoux, Bernard Rentier, Catherine Sadzot-Delvaux, and Jacques Piette

Department of Virology and Immunology, University of Liege, Liege, Liege B-4000

Corresponding Author: sbontems{at}ulg.ac.be

During the early phase of Varicella Zoster Virus (VZV) infection, Immediate Early protein 63 (IE63) is expressed rapidly and abundantly in the nucleus, while during latency, this protein is confined mostly to the cytoplasm. Since phosphorylation is known to regulate many cellular events, we investigated the importance of this modification on the cellular localization of IE63 and on its regulatory properties. We demonstrate here that cellular casein kinases I and II (CKI and CKII) are implicated in the in vitro and in vivo phosphorylation of IE63. A mutational approach also indicated that phosphorylation of the protein is important for its correct cellular localization in a cell-type dependent fashion. Using an activity test, we demonstrated that IE63 was able to repress the gene expression driven by two VZV promoters and that phosphorylation of the protein was required for its full repressive properties. Finally, we showed that IE63 was capable of exerting its repressive activity in the cytoplasm, as well as in the nucleus, suggesting a regulation at the transcriptional and/or post-transcriptional level.


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