| 1988 |
The CKA1 gene encodes the 42 kDa alpha catalytic subunit of yeast casein kinase II. Null disruption of CKA1 alone produces no detectable phenotype, indicating functional redundancy with the alpha' subunit encoded by CKA2. |
Gene cloning, sequencing, gene replacement/disruption in S. cerevisiae |
Molecular and cellular biology |
High |
3062376
|
| 1990 |
CKA1 and CKA2 together are essential for viability in S. cerevisiae; simultaneous deletion of both catalytic subunit genes is lethal. Loss of CKII activity causes cells to arrest with increased size, pseudomycelial morphology, and flocculation. Yeast lacking both subunits can be rescued by Drosophila CK2 alpha subunit alone or alpha+beta, demonstrating conservation of CK2 function across evolution. |
Gene replacement/disruption double mutant (cka1Δ cka2Δ), phenotypic analysis, cross-species complementation |
Molecular and cellular biology |
High |
2196445
|
| 1992 |
Casein kinase II forms an alpha2beta2 holoenzyme in vivo. In yeast rescued by Drosophila alpha alone, CK2 activity purifies as a free, catalytically active alpha subunit monomer; in yeast rescued by alpha+beta, it purifies as a mixture of tetrameric holoenzyme and monomeric alpha. Free catalytic subunit (overexpressed 6–18-fold) is not toxic in vivo. |
Biochemical purification and characterization of CK2 from rescued yeast strains, activity assays |
The Journal of biological chemistry |
High |
1527008
|
| 1998 |
The CKA1-encoded catalytic subunit has a distinct functional specialization from CKA2: cka1(ts) cka2 strains arrest with a nonpolarized actin cytoskeleton, delocalized chitin deposition, and multinucleate cells, establishing a requirement for CKII (specifically CKA1) in the maintenance of cell polarity in S. cerevisiae. |
Temperature-sensitive allele construction, conditional growth arrest, actin and chitin staining, cell morphology analysis |
The Journal of biological chemistry |
High |
9488724
|
| 1994 |
The human CSNK2A1 gene is located on chromosome 20p13. The gene contains at least 8 exons (covering bases 102–824 of the coding region), and introns contain tandemly arranged Alu repeats. |
Genomic library screening, FISH chromosomal localization, exon/intron mapping |
Genomics |
Medium |
8188256
|
| 1998 |
The complete human CSNK2A1 gene spans 70 kb, consists of 13 exons, has two transcription start sites, and its 5' promoter region shows housekeeping promoter features (no TATA box, CpG island, GC boxes). Reporter gene assay confirmed promoter activity between positions −256 and +144. |
Genomic cloning, primer extension, reporter gene assay |
Genomics |
Medium |
9503018
|
| 2011 |
The yeast CKA2 catalytic subunit phosphorylates C-terminal serines of the E2 ubiquitin-conjugating enzyme tmCdc34, and this phosphorylation prevents the synthesis of free polyubiquitin chains, likely by promoting their attachment to substrate. |
In vitro kinase assay, genetic epistasis (ubp14Δ, cka2Δ), polyubiquitination assays |
Cell division |
Medium |
21453497
|
| 2015 |
Yeast CKA2 is required for H2O2-induced apoptosis and high-temperature stress tolerance by regulating NOS-like-dependent nitric oxide (NO) accumulation; Δcka2 mutants show reduced NOS-like activity and reduced NO after H2O2 or high-temperature stress. |
Yeast deletion mutant (Δcka2), NO measurement, NOS-like activity assay, NO donor rescue experiment |
FEMS yeast research |
Medium |
26100262
|
| 2016 |
CSNK2A1 (CK2α) physically binds SIRT6 and phosphorylates it in vitro. Phosphorylation of SIRT6 at Ser338 by CSNK2A1 promotes breast cancer cell proliferation and invasiveness, and is required for nuclear β-catenin localization and upregulation of MMP9, β-catenin, cyclin D1, and NF-κB. |
Co-immunoprecipitation, GST pull-down assay, in vitro kinase assay, immunofluorescence, mutant CSNK2A1/SIRT6 transfection, siRNA knockdown |
The American journal of pathology |
High |
27746184
|
| 2021 |
CSNK2A1-mediated phosphorylation of SIRT6 at Ser338 activates the DNA damage repair pathway and confers doxorubicin resistance in osteosarcoma cells. Mutation of the SIRT6 Ser338 phosphorylation site attenuates CSNK2A1-mediated doxorubicin resistance in vivo. |
CSNK2A1 overexpression/knockdown, site-directed mutagenesis of SIRT6 Ser338, in vivo tumor models, Western blot |
Cells |
Medium |
34359939
|
| 2021 |
CSNK2A1 phosphorylates HMGA2 in a cisplatin-inducible manner. HMGA2 and CSNK2A1 co-localize in the nucleus and interact by co-immunoprecipitation. CX-4945 (CSNK2A1 inhibitor) blocks HMGA2 phosphorylation and sensitizes cervical cancer cells to cisplatin. |
Liquid chromatography–tandem mass spectrometry, co-immunoprecipitation, immunofluorescence co-localization, kinase inhibitor treatment |
FEBS open bio |
Medium |
34115920
|
| 2022 |
In S. pombe, the CK2α catalytic subunit Cka1 phosphorylates transcription cofactor PC4. This phosphorylation downregulates PC4's RNA polymerase II coactivator function; the CK2β regulatory subunit (Ckb1) inhibits this phosphorylation. Mutation of both CK2 consensus serine residues in PC4 abolishes phosphorylation and renders PC4 resistant to CK2α-mediated inactivation. |
In vitro phosphorylation assay, in vitro transcription assay, site-directed mutagenesis of PC4 serine residues |
International journal of molecular sciences |
High |
36012759
|
| 2022 |
Skeletal muscle-specific conditional knockout of CSNK2A1 in mice results in age-dependent grip strength reduction, impaired neuromuscular transmission, increased regenerating (central-nuclei) fibers, impaired oxidative metabolism with mitochondrial enzyme accumulation, stimulated autophagy, and fragmented neuromuscular junctions with increased synaptic gene expression. Ablation of CSNK2A1 also aberrantly changes protein levels of other CSNK2 subunits. |
Skeletal muscle-specific Cre-mediated conditional knockout (HSA-Cre), grip strength, electrophysiology, histology, enzyme activity, Western blot |
Cells |
High |
36552726
|
| 2023 |
CSNK2A1 phosphorylates MAX, shifting MAX-MAX homodimers to C-MYC-MAX and β-catenin-MAX heterodimers. These heterodimers increase HMGB1 and IL-6 promoter activities, promoting cholangiocarcinoma cell proliferation, migration, and invasion. |
Overexpression, co-immunoprecipitation, promoter activity assays, CK2 inhibitor (CX-4945) treatment, Western blot |
Hepatology communications |
Medium |
37347224
|
| 2023 |
CSNK2A1 competes with AKT1 to bind DUSP2 (dual-specificity phosphatase 2); this competition inhibits CSNK2A1-mediated phosphorylation of AKT1, promoting apoptosis in pancreatic cancer cells in an ERK1/2-independent manner. |
Co-immunoprecipitation, competition binding assays, in vitro and in vivo apoptosis assays, knockdown/overexpression |
Cancer letters |
Medium |
37390887
|
| 2024 |
Cholesterol directly binds to CSNK2A1, augmenting its kinase activity. Activated CSNK2A1 phosphorylates IGF2R at Ser2484, rewiring lipid-driven mitochondrial oxidative phosphorylation and generating reactive oxygen species, creating a positive feedback loop for cholesterol biosynthesis in hepatocellular carcinoma. |
Proteomics, phosphoproteomics, direct cholesterol-CSNK2A1 binding assay, kinase activity assay, patient-derived cell lines/organoids/xenografts |
Journal of advanced research |
Medium |
39547439
|
| 2024 |
OGT mediates O-GlcNAcylation of CSNK2A1, enhancing its protein stability. Knockdown of CSNK2A1 suppresses colorectal cancer cell proliferation, migration, invasion, and EMT; OGT overexpression reverses these effects in a CSNK2A1-dependent manner. |
Co-immunoprecipitation, Western blot, immunofluorescence, siRNA knockdown, in vivo tumor model |
Molecular biotechnology |
Medium |
38289573
|
| 2024 |
CSNK2A1 activates autophagy in pancreatic cancer cells, driving gemcitabine resistance. H3K27 acetylation mediates transcriptional regulation of CSNK2A1. The CSNK2A1 inhibitor Silmitasertib inhibits autophagy and restores gemcitabine sensitivity in vitro and in patient-derived xenograft models. |
siRNA knockdown, PDX model, autophagy assays, Silmitasertib pharmacological inhibition, bioinformatic analyses |
Cancer letters |
Medium |
38290659
|
| 2025 |
SOX4 transcriptionally upregulates CSNK2A1 by binding its promoter. CSNK2A1 in turn phosphorylates TOP2A, promoting breast cancer cell proliferation, migration, invasion, and tumor growth. Silencing SOX4 reduces CSNK2A1 expression and TOP2A phosphorylation. |
Dual-luciferase reporter assay, chromatin immunoprecipitation (ChIP), Western blot for phosphorylated TOP2A, siRNA knockdown, in vivo mouse tumor models |
FASEB journal |
Medium |
39931818
|
| 2025 |
In S. pombe, the CK2α catalytic subunit Cka1 physically associates with components of RSC chromatin remodeling complex, Pcs1/Mde4 (monopolin) complex, snoRNA-containing ribonucleoproteins, and spliceosomal machinery. In vitro kinase assays show Cka1 directly phosphorylates Pcs1 and Mde4. |
RNase-free tandem affinity purification coupled with mass spectrometry, in vitro kinase assay |
Biochemical and biophysical research communications |
Medium |
40700808
|
| 2025 |
A CSNK2A1 frameshift variant (c.1020_1021delAG, p.Gly342Glnfs*57) does not impair kinase activity in vitro but results in significantly reduced protein expression relative to wild-type, associated with elevated ubiquitination of the mutant protein. |
In vitro kinase assay, Western blot quantification, ubiquitination assay, overexpression of wild-type and mutant plasmids |
Frontiers in genetics |
Medium |
41216289
|