Casein kinases

Pyerin, Walter; and, Karin Ackermann; Lorenz, Peter

doi:10.1002/9783527615032.ch4

Cited by 15 publications

(3 citation statements)

References 110 publications

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“…The gene spans 70 kb and con-transduction (for reviews see Pinna, 1990; Tuazon and sists of 13 exons, and the exon/intron boundaries con- Traugh, 1991;Pyerin et al, 1996). Of main interest are form to the gt/ag rule.…”

mentioning

confidence: 99%

Genomic Organization and Promoter Identification of the Human Protein Kinase CK2 Catalytic Subunit α (CSNK2A1)

et al. 1998

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confidence: 99%

Genomic Organization and Promoter Identification of the Human Protein Kinase CK2 Catalytic Subunit α (CSNK2A1)

et al. 1998

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“…However, CK2 has been linked to proliferation, transformation, and cell cycle regulation (reviewed in Refs. [1][2][3][4][5][6][7][8][9][10].…”

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Transcription Factors Ets1, NF-κB, and Sp1 Are Major Determinants of the Promoter Activity of the Human Protein Kinase CK2α Gene

Krehan¹,

Ansuini²,

Böcher³

et al. 2000

Journal of Biological Chemistry

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CK2␣ is one of two isoforms of protein kinase CK2, a highly conserved, ubiquitous, and vital phosphotransferase whose expression is kept at constant cellular levels and whose dysregulated expression has been linked to malignant diseases. The upstream sequence of the gene coding for human CK2␣ (CSNK1A1, chromosomal location 20p13) has been examined for promoter location and transcription factor interactions using reporter gene assays (luciferase; HeLa cells), site-directed mutagenesis, electrophoretic mobility shift assays, super-shifts, UV cross-linking, Western blotting, and DNA affinity chromatography. Highest promoter activity has been found in a region comprising positions ؊9 to 46. Factors Sp1, Ets-1, and NF-B have been identified as interaction partners and, by mutation of individual sites and simultaneous mutations of two or more sites, shown to cross-talk to each other. At least two of the factors (Sp1; NF-B) were susceptible to phosphorylation by CK2 holoenzyme, a tetramer composed of two CK2␣ and two regulatory CK2␤ proteins, but not by individual CK2␣. Because the phosphorylation decreases promoter binding and repeated immunoprecipitation reveals presence of "free" CK2␤ in cell extracts, it is tempting to speculate that the gene product CK2␣ might readily form CK2 holoenzyme and feed back onto gene transcription. The data represent the first promoter control analysis of a mammalian CK2␣ gene and provide a hypothesis of how the constant expression level of CK2␣ may be achieved. Protein kinase CK21 (also named casein kinase II) is a pleiotropic, ubiquitous, and conserved Ser/Thr kinase that is essential for viability of eukaryotes. CK2 occurs in two highly related isoforms, CK2␣ and CK2␣Ј. Both of these occur as tetrameric holoenzymes complexed stoichiometrically to regulatory CK2␤ proteins. This tetrameric structure is also highly conserved and required for appropriate control of substrate specificity. Although a considerable number of substrates has been documented, comprising proteins involved in processes such as transcription, replication, translation, and signaling, the exact physiological role of CK2 remains poorly understood. However, CK2 has been linked to proliferation, transformation, and cell cycle regulation (reviewed in Refs.

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“…This could be the serine that is phosphorylated, but beyond the fact of its conservation, the evidence supporting this hypothesis is no more than suggestive. The sequence around this serine in the L18 from B. stearothermophilus and from many other eubacteria L18's (Figure 1, see 7) is the same as the sequence recognized by a eukaryotic protein kinase, casein kinase II (CKII), which recognizes the motif -X-Ser/Thr-X-X-Asp/Glu- (21). Interestingly, the ribosomal protein that binds 5S rRNA in humans, L5 (22), which includes sequences homologous to prokaryotic L18 (23), interacts with the β subunit of CKII (24), and its chicken homologue binds to protein phosphatase PP1 (25).…”

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confidence: 90%

Phosphorylation of Ribosomal Protein L18 Is Required for Its Folding and Binding to 5S rRNA

Bloemink

Moore

1999

Biochemistry

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Ribosomal protein L18 from Bacillus stearothermophilus (bL18) includes a previously unreported phosphoserine residue. The folded conformation of the protein is stabilized by the dianionic form of the phosphate group of that residue. In the absence of Mg2+, the pK(a) of the phosphate group is so high that the protein is not fully folded at pH 7. In the presence of Mg2+, its pK(a) drops significantly, and consequently the native conformation of bL18 becomes stable at pH 7 and the protein is able to bind to 5S rRNA. Dephosphorylated bL18 does not bind to 5S rRNA at neutral pH.

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Casein kinases

Cited by 15 publications

References 110 publications

Genomic Organization and Promoter Identification of the Human Protein Kinase CK2 Catalytic Subunit α (CSNK2A1)

Genomic Organization and Promoter Identification of the Human Protein Kinase CK2 Catalytic Subunit α (CSNK2A1)

Transcription Factors Ets1, NF-κB, and Sp1 Are Major Determinants of the Promoter Activity of the Human Protein Kinase CK2α Gene

Phosphorylation of Ribosomal Protein L18 Is Required for Its Folding and Binding to 5S rRNA

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