Protein kinase CK2 (formerly termed “casein kinase II”) is an extremely conserved
Ser/Thr kinase, which is ubiquitously distributed in eukaryotic cells. CK2 is quite
unique enzyme, strongly distinguished from others protein kinases by particularly
two properties—high constitutive activity and lack of an acute mechanism/s of regulation.
The extreme pleiotropy (with list of over 300 substrates) is another of its characteristic
[
[1]
]. Despite of the gaps in understanding of precise molecular mechanisms the importance
of CK2 in the context of signal transduction, gene expression and respectively in
the cell regulation, including the maintenance of cell cycle is incontestable.To read this article in full you will need to make a payment
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References
- One-thousand-and-one substrates of protein kinase CK2?.FASEB J. 2003; 17 (349 368)
- Distinct and overlapping roles for E2F family members in transcription, proliferation and apoptosis.Curr Mol Med. 2006; 6 (739 748)
- The regulation of E2F by pRB-family proteins.Genes Dev. 1998; 12 (2245 2262)
- A novel mechanism of E2F1 regulation via nucleocytoplasmic shuttling. Determinants of nuclear import and export.Cell Cycle. 2007; 6 (2186 2195)
- c-Myc-regulated microRNAs modulate E2F1 expression.Nature. 2005; 435 (839843)
- Proteins of the Myc network: essential regulators of cell growth and differentiation.Adv Cancer Res. 1996; 68 (109 182)
- Control of E2F activity by p21Waf1/Cip1.Oncogene. 1999; 18 (381 5392)
- Activation of p38- and CRM1-dependent nuclear export promotes E2F1 degradation during keratinocyte differentiation.Oncogene. 2007; 26 (1147 1154)
- Inhibition of CK2 activity provokes opposite effects on ERK1/2 phosphorylation and p38 MAPK phosphorylation in normal human keratinocytes.Compt Rend Acad Bulg Sci. 2007; 60 (909 912)
- Protein p21WAF1/CIP1 is phosphorylated by protein kinase CK2 in vitro and interacts with the amino terminal end of the CK2 beta subunit.J Cell Biochem. 2001; 81 (445 452)
Article info
Publication history
Published online: July 12, 2010
Received:
January 20,
2009
Identification
Copyright
© 2009 Japanese Society for Investigative Dermatology. Published by Elsevier Inc. All rights reserved.
