A N-terminally deleted form of the CK2α' catalytic subunit is sufficient to support cell viability.
Biochem Biophys Res Commun
; 531(3): 409-415, 2020 10 20.
Article
em En
| MEDLINE
| ID: mdl-32800562
ABSTRACT
Viable clones of C2C12 myoblasts where both catalytic subunits of protein kinase CK2 had been knocked out by the CRISPR/Cas9 methodology have recently been generated, thus challenging the concept that CK2 is essential for cell viability. Here we present evidence that these cells are still endowed with a residual "CK2-like" activity that is able to phosphorylate Ser-13 of endogenous CDC37. Searching for a molecular entity accounting for such an activity we have identified a band running slightly ahead of CK2α' on SDS-PAGE. This band is not detectable by in-gel casein kinase assay but it co-immuno-precipitates with the ß-subunit being downregulated by specific CK2α' targeting siRNA treatment. Its size and biochemical properties are consistent with those of CK2α' mutants deleted upstream of Glu-15 generated during the knockout process. This mutant sheds light on the role of the CK2 N-terminal segment as a regulator of activity and stability. Comparable cytotoxic efficacy of two selective and structurally unrelated CK2 inhibitors support the view that survival of CK2α/α'-/- cells relies on this deleted form of CK2α', whose discovery provides novel perspectives about the biological role of CK2.
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Texto completo:
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Base de dados:
MEDLINE
Assunto principal:
Deleção de Sequência
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Domínio Catalítico
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Caseína Quinase II
Limite:
Animals
Idioma:
En
Ano de publicação:
2020
Tipo de documento:
Article