Comparison of varicella-zoster virus ORF47 protein kinase and casein kinase II and their substrates

2003 ◽  
Vol 70 (S1) ◽  
pp. S95-S102 ◽  
Author(s):  
T.K. Kenyon ◽  
Elizabeth Homan ◽  
J. Storlie ◽  
Minako Ikoma ◽  
Charles Grose
Keyword(s):  
Protein Kinase ◽  
Varicella Zoster Virus ◽  
Casein Kinase Ii ◽  
Casein Kinase ◽  
Varicella Zoster

scholarly journals Varicella-Zoster Virus Fc Receptor Component gI Is Phosphorylated on Its Endodomain by a Cyclin-Dependent Kinase

1999 ◽  
Vol 73 (2) ◽  
pp. 1320-1330 ◽  
Author(s):  
Ming Ye ◽  
Karen M. Duus ◽  
Junmin Peng ◽  
David H. Price ◽  
Charles Grose
Keyword(s):  
Fusion Protein ◽  
Varicella Zoster Virus ◽  
Phosphorylation Site ◽  
Cytoplasmic Tail ◽  
Casein Kinase Ii ◽  
Fc Receptor ◽  
Casein Kinase ◽  
Cyclin Dependent Kinase ◽  
Varicella Zoster

Varicella-zoster virus (VZV) glycoprotein gI is a type 1 transmembrane glycoprotein which is one component of the heterodimeric gE:gI Fc receptor complex. Like VZV gE, VZV gI was phosphorylated in both VZV-infected cells and gI-transfected cells. Preliminary studies demonstrated that a serine 343-proline 344 sequence located within the gI cytoplasmic tail was the most likely phosphorylation site. To determine which protein kinase catalyzed the gI phosphorylation event, we constructed a fusion protein, consisting of glutathione-S-transferase (GST) and the gI cytoplasmic tail, called GST-gI-wt. When this fusion protein was used as a substrate for gI phosphorylation in vitro, the results demonstrated that GST-gI-wt fusion protein was phosphorylated by a representative cyclin-dependent kinase (CDK) called P-TEFb, a homologue of CDK1 (cdc2). When serine 343 within the serine-proline phosphorylation site was replaced with an alanine residue, the level of phosphorylation of the gI fusion protein was greatly reduced. Subsequent experiments with individually immunoprecipitated mammalian CDKs revealed that the VZV gI fusion protein was phosphorylated best by CDK1, to a lesser degree by CDK2, and not at all by CDK6. Transient-transfection assays carried out in the presence of the specific CDK inhibitor roscovitine strongly supported the prior results by demonstrating a marked decrease in gI phosphorylation while gI protein expression was unaffected. Finally, the possibility that VZV gI contained a CDK phosphorylation site in its endodomain was of further interest because its partner, gE, contains a casein kinase II phosphorylation site in its endodomain; prior studies have established that CDK1 can phosphorylate casein kinase II.

scholarly journals Phosphorylation of the Nuclear Form of Varicella-Zoster Virus Immediate-Early Protein 63 by Casein Kinase II at Serine 186

2009 ◽  
Vol 83 (23) ◽  
pp. 12094-12100 ◽  
Author(s):  
Niklaus H. Mueller ◽  
Laurie L. Graf ◽  
David Orlicky ◽  
Don Gilden ◽  
Randall J. Cohrs
Keyword(s):  
Monoclonal Antibody ◽  
Varicella Zoster Virus ◽  
Casein Kinase Ii ◽  
Casein Kinase ◽  
Antibody Binding ◽  
Immediate Early ◽  
Productive Infection ◽  
Varicella Zoster ◽  
Recombinant Monoclonal Antibody ◽  
Early Protein

ABSTRACT Varicella-zoster virus (VZV) open reading frame (ORF) 63 is abundantly transcribed in latently infected human ganglia and encodes a 278-amino-acid protein, IE63, with immediate-early kinetics. IE63 is expressed in the cytoplasm of neurons during VZV latency and in both the cytoplasm and the nucleus during productive infection; however, the mechanism(s) involved in IE63 nuclear import and retention has remained unclear. We constructed and identified a recombinant monoclonal antibody to detect a posttranslationally modified form of IE63. Analysis of a series of IE63 truncation and substitution mutants showed that amino acids 186 to 195 are required for antibody binding. Synthetic peptides corresponding to this region identified IE63 S186 as a target for casein kinase II phosphorylation. In addition, acidic charges supplied by E194 and E195 were required for antibody binding. Immunofluorescence analysis of VZV-infected MeWo cells using the recombinant monoclonal antibody detected IE63 exclusively in the nuclei of infected cells, indicating that casein kinase II phosphorylation of S186 occurs in the nucleus and possibly identifying an initial molecular event operative in VZV reactivation.

Inhibition of protein kinase C- and casein kinase II-mediated phosphorylation of GAP-43 by S100β

1994 ◽  
Vol 25 (3-4) ◽  
pp. 297-304 ◽  
Author(s):  
Li-Hsien Lin ◽  
Linda J. Van Eldik ◽  
Neil Osheroff ◽  
Jeanette J. Norden
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Casein Kinase Ii ◽  
Casein Kinase ◽  
Kinase C

Identification of Glycyrrhizin-Binding Protein Kinase as Casein Kinase II and Characterization of Its Associated Phosphate Acceptors in Mouse Liver

1996 ◽  
Vol 227 (1) ◽  
pp. 102-109 ◽  
Author(s):  
Shigeyoshi Harada ◽  
Atsushi Karino ◽  
Yoshihito Shimoyama ◽  
Fazel Shamsa ◽  
Kenzo Ohtsuki
Keyword(s):  
Protein Kinase ◽  
Mouse Liver ◽  
Binding Protein ◽  
Casein Kinase Ii ◽  
Casein Kinase

Nucleoplasmin associates with and is phosphorylated by casein kinase II

1995 ◽  
Vol 108 (2) ◽  
pp. 779-787 ◽  
Author(s):  
I. Vancurova ◽  
T.M. Paine ◽  
W. Lou ◽  
P.L. Paine
Keyword(s):  
Protein Kinase ◽  
Polyclonal Antibody ◽  
Nuclear Transport ◽  
Specific Inhibitor ◽  
Casein Kinase Ii ◽  
Casein Kinase ◽  
Transferase Activity ◽  
Catalytic Subunits ◽  
Kinetics Of

Nucleoplasmin is a phosphorylated nuclear-accumulating protein. We report herein that the kinetics of its cytoplasm-->nucleus transport are affected by its degree of phosphorylation. Therefore, we sought to identify any protein kinase which specifically associates with nucleoplasmin. We discovered that nucleoplasmin co-isolates by two independent methods (immunoabsorption and chromatography) in a complex including a kinase which phosphorylates nucleoplasmin. The co-purifying kinase is casein kinase II-like because: (i) it phosphorylates casein; (ii) its phospho-transferase activity can be competed out by GTP; (iii) it is stimulated by polylysine; and (iv) it is inhibited by heparin. Moreover, a polyclonal antibody to the alpha (38 kDa) and alpha' (36 kDa) catalytic subunits of casein kinase II specifically recognizes 38 and 36 kDa polypeptides in the nucleoplasmin-complex, and a specific inhibitor of casein kinase II inhibits nucleoplasmin's nuclear transport. Additionally, we found that phosphorylation of nucleoplasmin by its associated casein kinase II is strongly inhibited by histones and that, in addition to nucleoplasmin, another protein (p100) in the nucleoplasmin-complex is phosphorylated by casein kinase II.

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