Next Article in Journal
Aptamers in Bordeaux, 24–25 June 2016
Next Article in Special Issue
CK2 in Cancer: Cellular and Biochemical Mechanisms and Potential Therapeutic Target
Previous Article in Journal / Special Issue
Ablation of Protein Kinase CK2β in Skeletal Muscle Fibers Interferes with Their Oxidative Capacity
Article Menu
Issue 1 (March) cover image

Export Article

Open AccessReview
Pharmaceuticals 2017, 10(1), 11; doi:10.3390/ph10010011

Exploring the CK2 Paradox: Restless, Dangerous, Dispensable

1
Department of Biomedical Sciences, University of Padova, via U. Bassi, 58/B, 35131 Padova, Italy
2
Proteomics Center, University of Padova and Azienda Ospedaliera di Padova, via G. Orus, 2/B, 35129 Padova, Italy
3
CNR Neurosciences Institute, via U. Bassi, 58/B, 35131 Padova, Italy
*
Author to whom correspondence should be addressed.
Academic Editor: Marc Le Borgne
Received: 28 November 2016 / Revised: 12 January 2017 / Accepted: 16 January 2017 / Published: 20 January 2017
View Full-Text   |   Download PDF [1090 KB, uploaded 3 February 2017]   |  

Abstract

The history of protein kinase CK2 is crowded with paradoxes and unanticipated findings. Named after a protein (casein) that is not among its physiological substrates, CK2 remained in search of its targets for more than two decades after its discovery in 1954, but it later came to be one of the most pleiotropic protein kinases. Being active in the absence of phosphorylation and/or specific stimuli, it looks unsuitable to participate in signaling cascades, but its “lateral” implication in a variety of signaling pathways is now soundly documented. At variance with many “onco-kinases”, CK2 is constitutively active, and no oncogenic CK2 mutant is known; still high CK2 activity correlates to neoplasia. Its pleiotropy and essential role may cast doubts on the actual “druggability” of CK2; however, a CK2 inhibitor is now in Phase II clinical trials for the treatment of cancer, and cell clones viable in the absence of CK2 are providing information about the mechanism by which cancer becomes addicted to high CK2 levels. A phosphoproteomics analysis of these CK2 null cells suggests that CK2 pleiotropy may be less pronounced than expected and supports the idea that the phosphoproteome generated by this kinase is flexible and not rigidly pre-determined. View Full-Text
Keywords: protein kinase CK2; casein kinase 2; cancer; signal transduction; non oncogene addiction; phosphoproteomics; CRISPR/Cas9 technology protein kinase CK2; casein kinase 2; cancer; signal transduction; non oncogene addiction; phosphoproteomics; CRISPR/Cas9 technology
Figures

Figure 1

This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

Scifeed alert for new publications

Never miss any articles matching your research from any publisher
  • Get alerts for new papers matching your research
  • Find out the new papers from selected authors
  • Updated daily for 49'000+ journals and 6000+ publishers
  • Define your Scifeed now

SciFeed Share & Cite This Article

MDPI and ACS Style

Franchin, C.; Borgo, C.; Zaramella, S.; Cesaro, L.; Arrigoni, G.; Salvi, M.; Pinna, L.A. Exploring the CK2 Paradox: Restless, Dangerous, Dispensable. Pharmaceuticals 2017, 10, 11.

Show more citation formats Show less citations formats

Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Related Articles

Article Metrics

Article Access Statistics

1

Comments

[Return to top]
Pharmaceuticals EISSN 1424-8247 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top