CK2 Protein Kinase Is Stimulated and Redistributed by Functional Herpes Simplex Virus ICP27 Protein
Open Access
- 1 April 2003
- journal article
- Published by American Society for Microbiology in Journal of Virology
- Vol. 77 (7), 4315-4325
- https://doi.org/10.1128/jvi.77.7.4315-4325.2003
Abstract
It has been shown previously (S. Wadd, H. Bryant, O. Filhol, J. E. Scott, T.-T. Hsieh, R. D. Everett, and J. B. Clements, J. Biol. Chem. 274:28991-28998, 2000) that ICP27, an essential and multifunctional herpes simplex virus type 1 (HSV-1) protein, interacts with CK2 and with heterogeneous ribonucleoprotein K (hnRNP K). CK2 is a pleiotropic and ubiquitous protein kinase, and the tetrameric holoenzyme consists of two catalytic α or α′ subunits and two regulatory β subunits. We show here that HSV-1 infection stimulates CK2 activity. CK2 stimulation occurs at early times after infection and correlates with redistribution of the holoenzyme from the nucleus to the cytoplasm. Both CK2 stimulation and redistribution require expression and cytoplasmic accumulation of ICP27. In HSV-1-infected cells, CK2 phosphorylates ICP27 and affects its cytoplasmic accumulation while it also phosphorylates hnRNP K, which is not ordinarily phosphorylated by this kinase, suggesting an alteration of hnRNP K activities. This is the first example of CK2 stimulation by a viral protein in vivo, and we propose that it might facilitate the HSV-1 lytic cycle by, for example, regulating trafficking of ICP27 protein and/or viral RNAs.Keywords
This publication has 51 references indexed in Scilit:
- Association of Herpes Simplex Virus Type 1 ICP8 and ICP27 Proteins with Cellular RNA Polymerase II HoloenzymeJournal of Virology, 2002
- Herpes Simplex Virus Type 1 Blocks the Apoptotic Host Cell Defense Mechanisms That Target Bcl-2 and Manipulates Activation of p38 Mitogen-Activated Protein Kinase To Improve Viral ReplicationJournal of Virology, 2001
- Subcellular localization of protein kinase CK2Cell and tissue research, 2000
- Stress-induced Activation of Protein Kinase CK2 by Direct Interaction with p38 Mitogen-activated Protein KinasePublished by Elsevier BV ,2000
- DNA damage triggers DRB-resistant phosphorylation of human p53 at the CK2 siteOncogene, 1998
- Posttranscriptional Regulation in Herpes Simplex VirusSeminars in Virology, 1998
- The carboxy terminus of p53 mimics the polylysine effect of protein kinase CK2-catalyzed MDM2 phosphorylationOncogene, 1997
- Oligomeric Casein Kinase II Isoforms Are Expressed in Bovine Tissues and Adrenocortical Cells in CultureBiochemical and Biophysical Research Communications, 1994
- Shuttling of pre-mRNA binding proteins between nucleus and cytoplasmNature, 1992
- Herpes simplex virus induces a processing factor that stimulates poly(A) site usageCell, 1989