Depletion of catalytic and regulatory subunits of protein kinase CK2 by antisense oligonucleotide treatment of neuroblastoma cells

1994 ◽  
Vol 14 (5) ◽  
pp. 407-414 ◽  
Author(s):  
Luis Ulloa ◽  
Javier Díaz-Nido ◽  
Jesus Avila
2009 ◽  
Vol 54 (2) ◽  
pp. 220-226 ◽  
Author(s):  
WeiHong Zhou ◽  
XiaoHong Qin ◽  
XiaoJie Yan ◽  
XingQiao Xie ◽  
Liang Li ◽  
...  

2006 ◽  
Vol 295 (1-2) ◽  
pp. 229-236 ◽  
Author(s):  
Konrad Kubiński ◽  
Katarzyna Domańska ◽  
Ewa Sajnaga ◽  
Elżbieta Mazur ◽  
Rafał Zieliński ◽  
...  

2001 ◽  
Vol 358 (1) ◽  
pp. 87-94 ◽  
Author(s):  
David A. CANTON ◽  
Cunjie ZHANG ◽  
David W. LITCHFIELD

Protein kinase CK2 is a tetrameric enzyme comprised of two regulatory subunits (CK2β) and two catalytic subunits (CK2α and/or CK2α′). The crystal structure of dimeric CK2β demonstrated that a zinc finger mediates CK2β dimerization, therefore we constructed a mutant in which cysteine residues 109 and 114 were mutated to serine. Our objectives were to examine the effects of disrupting the zinc finger of the regulatory CK2β subunit on CK2 tetramer assembly. Examination of this zinc-finger-deficient mutant of CK2β using a yeast two-hybrid assay demonstrates that the mutant fails to form CK2β homodimers. In order to extend these studies, we co-transfected COS-7 cells with epitope-tagged constructs and performed co-immunoprecipitation assays. The results from these studies demonstrate that the mutant fails to form CK2β homodimers and fails to interact with catalytic CK2 subunits. Furthermore, we demonstrate that the mutant CK2β is not appreciably phosphorylated in cells. Using in vitro binding assays, we demonstrated that the mutant CK2β protein fails to interact with glutathione S-transferase–CK2α′. Finally, we demonstrate that the mutant is translated at an equivalent rate to wild-type CK2β, but is degraded much more rapidly. Overall, our results are consistent with the model that β–β dimerization precedes incorporation of catalytic subunits into tetrameric CK2 complexes, and that β–β dimerization is a prerequisite for the stable incorporation of catalytic subunits into CK2 complexes.


2007 ◽  
Vol 28 (1) ◽  
pp. 131-139 ◽  
Author(s):  
David Y. Lou ◽  
Isabel Dominguez ◽  
Paul Toselli ◽  
Esther Landesman-Bollag ◽  
Conor O'Brien ◽  
...  

ABSTRACT Protein kinase CK2 (formerly casein kinase II) is a highly conserved and ubiquitous serine/threonine kinase that is composed of two catalytic subunits (CK2α and/or CK2α′) and two CK2β regulatory subunits. CK2 has many substrates in cells, and key roles in yeast cell physiology have been uncovered by introducing subunit mutations. Gene-targeting experiments have demonstrated that in mice, the CK2β gene is required for early embryonic development, while the CK2α′ subunit appears to be essential only for normal spermatogenesis. We have used homologous recombination to disrupt the CK2α gene in the mouse germ line. Embryos lacking CK2α have a marked reduction in CK2 activity in spite of the presence of the CK2α′ subunit. CK2α−/− embryos die in mid-gestation, with abnormalities including open neural tubes and reductions in the branchial arches. Defects in the formation of the heart lead to hydrops fetalis and are likely the cause of embryonic lethality. Thus, CK2α appears to play an essential and uncompensated role in mammalian development.


2001 ◽  
Vol 25 (4) ◽  
pp. 365-374 ◽  
Author(s):  
Marta Riera ◽  
Giovanna Peracchia ◽  
Eulàlia De Nadal ◽  
Joaquín Ariño ◽  
Montserrat Pagès

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