The DOI matches its Crossref record; 29 of the 29 references it cites were found in a registry or an index.
Protein kinase CK2: a challenge to canons
Abstract
CK2 is an extremely conserved pleiotropic protein kinase with a growing list of more than 300 substrates, the majority of which are proteins implicated in signal transduction, gene expression and other nuclear functions. The CK2 phosphoacceptor sites are specified by multiple acidic residues, with the one at position +3 relative to the target residue being of crucial relevance. The CK2 holoenzyme is composed of two catalytic subunits(αα, α′α′ or αα′), which are essential for cell viability, and a dimer of two non-catalytic βsubunits, whose precise function is still poorly understood. Although theβ subunits deeply affect many properties of CK2, both the isolated catalytic subunits and the holoenzyme are constitutively active, which is probably responsible for the oncogenic potential of CK2. Given the structure of the holoenzyme, the β subunits could undergo reversible dissociation under physiological conditions and play a role as anchoring elements and/or as a docking platform for protein substrates and effectors. These unusual features are likely to be instrumental in the involvement of CK2 in a number of key biological functions, notably RNA synthesis, Wnt signaling,ubiquitination and cell survival.
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Cites
Functional organization of the yeast proteome by systematic analysis of protein complexes
Gavin, A.-C., Bösche, M., Krause, R., Grandi, P., Marzioch, M., Bauer, A., Schultz, J., Rick, J. M., Michon, A.-M., Cruciat, C.-M., et al. (2002) · Nature · doi:10.1038/415141a · Cited by 4,759
Blume-Jensen, P., & Hunter, T. (2001) · Nature · doi:10.1038/35077225 · Cited by 3,738
Systematic identification of protein complexes in Saccharomyces cerevisiae by mass spectrometry
Ho, Y., Gruhler, A., Heilbut, A., Bader, G. D., Moore, L., Adams, S.-L., Millar, A., Taylor, P., Bennett, K., Boutilier, K., et al. (2002) · Nature · doi:10.1038/415180a · Cited by 3,601
Casein kinase 2: An ‘eminence grise’ in cellular regulation?
Pinna, L. A. (1990) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/0167-4889(90)90098-x · Cited by 906
Self-citationCrystal structure of human protein kinase CK2: insights into basic properties of the CK2 holoenzyme
Niefind, K. (2001) · The EMBO Journal · doi:10.1093/emboj/20.19.5320 · Cited by 444
Casein Kinase IIα Transgene-Induced Murine Lymphoma: Relation to Theileriosis in Cattle
Seldin, D. C., & Leder, P. (1995) · Science · doi:10.1126/science.7846532 · Cited by 395
Protein kinase CK2 and its role in cellular proliferation, development and pathology
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Self-citationPadmanabha, R., Chen-Wu, J. L., Hanna, D. E., & Glover, C. V. (1990) · Molecular and Cellular Biology · doi:10.1128/mcb.10.8.4089 · Cited by 354
Phosphorylation of Bid by Casein Kinases I and II Regulates Its Cleavage by Caspase 8
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Cited by
One‐thousand‐and‐one substrates of protein kinase CK2?
Meggio, F., & Pinna, L. A. (2003) · The FASEB Journal · doi:10.1096/fj.02-0473rev · Cited by 1,310
Self-citationChen, G., Han, Z., Feng, D., Chen, Y., Chen, L., Wu, H., Huang, L., Zhou, C., Cai, X., Fu, C., et al. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.02.034 · Cited by 599
Protein Kinase CK2 in Health and Disease: CK2: A key player in cancer biology
Trembley, J. H., Wang, G., Unger, G., Slaton, J., & Ahmed, K. (2009) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-009-9154-y · Cited by 354
Addiction to protein kinase CK2: A common denominator of diverse cancer cells?
Ruzzene, M., & Pinna, L. A. (2010) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2009.07.018 · Cited by 352
Self-citationWharton, K. A. (2003) · Developmental Biology · doi:10.1006/dbio.2002.0869 · Cited by 315
Metadata
- Authors
- Pinna, L. A.
- Venue
- Journal of Cell Science
- Publisher
- The Company of Biologists
- Published
- 2002-10-15
- Volume
- 115
- Issue
- 20
- Pages
- 3873-3878
- ISSN
- 0021-9533 (ISSN-L)
- 1477-9137
- OpenAlex
- W1973466091
- Cited by
- 492
- References
- 29
- FWCI
- 9.07
- Type
- journal article
- Language
- en
- Open access
- closed
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