CK2 Regulation: Perspectives in 2021
The protein kinase CK2 (CK2) family encompasses a small number of acidophilic serine/threonine kinases that phosphorylate substrates involved in numerous biological processes including apoptosis, cell proliferation, and the DNA damage response. CK2 has also been implicated in many human malignancies...
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| Format: | Article |
| Language: | English |
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MDPI AG
2021-09-01
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| Series: | Biomedicines |
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| Online Access: | https://www.mdpi.com/2227-9059/9/10/1361 |
| _version_ | 1797515226729414656 |
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| author | Scott E. Roffey David W. Litchfield |
| author_facet | Scott E. Roffey David W. Litchfield |
| author_sort | Scott E. Roffey |
| collection | DOAJ |
| description | The protein kinase CK2 (CK2) family encompasses a small number of acidophilic serine/threonine kinases that phosphorylate substrates involved in numerous biological processes including apoptosis, cell proliferation, and the DNA damage response. CK2 has also been implicated in many human malignancies and other disorders including Alzheimer′s and Parkinson’s diseases, and COVID-19. Interestingly, no single mechanism describes how CK2 is regulated, including activation by external proteins or domains, phosphorylation, or dimerization. Furthermore, the kinase has an elongated activation loop that locks the kinase into an active conformation, leading CK2 to be labelled a constitutively active kinase. This presents an interesting paradox that remains unanswered: how can a constitutively active kinase regulate biological processes that require careful control? Here, we highlight a selection of studies where CK2 activity is regulated at the substrate level, and discuss them based on the regulatory mechanism. Overall, this review describes numerous biological processes where CK2 activity is regulated, highlighting how a constitutively active kinase can still control numerous cellular activities. It is also evident that more research is required to fully elucidate the mechanisms that regulate CK2 and what causes aberrant CK2 signaling in disease. |
| first_indexed | 2024-03-10T06:42:31Z |
| format | Article |
| id | doaj.art-811b51df9c0c4e248faeed8f41db0cbc |
| institution | Directory Open Access Journal |
| issn | 2227-9059 |
| language | English |
| last_indexed | 2024-03-10T06:42:31Z |
| publishDate | 2021-09-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Biomedicines |
| spelling | doaj.art-811b51df9c0c4e248faeed8f41db0cbc2023-11-22T17:30:41ZengMDPI AGBiomedicines2227-90592021-09-01910136110.3390/biomedicines9101361CK2 Regulation: Perspectives in 2021Scott E. Roffey0David W. Litchfield1Department of Biochemistry, Schulich School of Medicine & Dentistry, University of Western Ontario, London, ON N6A 5C1, CanadaDepartment of Biochemistry, Schulich School of Medicine & Dentistry, University of Western Ontario, London, ON N6A 5C1, CanadaThe protein kinase CK2 (CK2) family encompasses a small number of acidophilic serine/threonine kinases that phosphorylate substrates involved in numerous biological processes including apoptosis, cell proliferation, and the DNA damage response. CK2 has also been implicated in many human malignancies and other disorders including Alzheimer′s and Parkinson’s diseases, and COVID-19. Interestingly, no single mechanism describes how CK2 is regulated, including activation by external proteins or domains, phosphorylation, or dimerization. Furthermore, the kinase has an elongated activation loop that locks the kinase into an active conformation, leading CK2 to be labelled a constitutively active kinase. This presents an interesting paradox that remains unanswered: how can a constitutively active kinase regulate biological processes that require careful control? Here, we highlight a selection of studies where CK2 activity is regulated at the substrate level, and discuss them based on the regulatory mechanism. Overall, this review describes numerous biological processes where CK2 activity is regulated, highlighting how a constitutively active kinase can still control numerous cellular activities. It is also evident that more research is required to fully elucidate the mechanisms that regulate CK2 and what causes aberrant CK2 signaling in disease.https://www.mdpi.com/2227-9059/9/10/1361protein kinase CK2casein kinase IICSNK2phosphorylationpost-translational modificationssignal transduction |
| spellingShingle | Scott E. Roffey David W. Litchfield CK2 Regulation: Perspectives in 2021 Biomedicines protein kinase CK2 casein kinase II CSNK2 phosphorylation post-translational modifications signal transduction |
| title | CK2 Regulation: Perspectives in 2021 |
| title_full | CK2 Regulation: Perspectives in 2021 |
| title_fullStr | CK2 Regulation: Perspectives in 2021 |
| title_full_unstemmed | CK2 Regulation: Perspectives in 2021 |
| title_short | CK2 Regulation: Perspectives in 2021 |
| title_sort | ck2 regulation perspectives in 2021 |
| topic | protein kinase CK2 casein kinase II CSNK2 phosphorylation post-translational modifications signal transduction |
| url | https://www.mdpi.com/2227-9059/9/10/1361 |
| work_keys_str_mv | AT scotteroffey ck2regulationperspectivesin2021 AT davidwlitchfield ck2regulationperspectivesin2021 |