ArticleCurrent genetics2006
A specific catalytic subunit isoform of protein kinase CK2 is required for phosphorylation of the repressor Nrg1 in Saccharomyces cerevisiae.
Article in Current genetics, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 19 citations in OpenAlex.
- Recurrent sequence evolution after independent gene duplication.BMC evolutionary biology · 2020Article
- Predicting CK2 beta-dependent substrates using linear patterns.Biochemistry and biophysics reports · 2015Article
- Coupling mRNA synthesis and decay.Molecular and cellular biology · 2014Review
- Casein kinase 2 is essential for mitophagy.EMBO reports · 2013Article
- Predominance of CK2α over CK2α' in the mammalian brain.Molecular and cellular biochemistry · 2011Article
- Suppression of Ycf1p function by Cka1p-dependent phosphorylation is attenuated in response to salt stress.FEMS yeast research · 2010Article
- ESCRT-III protein Snf7 mediates high-level expression of the SUC2 gene via the Rim101 pathway.Eukaryotic cell · 2008Article
- Function and regulation of the Saccharomyces cerevisiae ENA sodium ATPase system.Eukaryotic cell · 2007Article
- Mechanisms regulating the protein kinases of Saccharomyces cerevisiae.Eukaryotic cell · 2007Review
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Protein kinase CK2 is highly conserved in eukaryotes and plays roles in many different cellular processes. CK2 is a tetramer comprising two catalytic and two regulatory subunits. Most organisms have two major isoforms of the catalytic subunit, and evidence suggests strongly overlapping function. In the yeast Saccharomyces cerevisiae, CK2 is essential for viability, and either catalytic subunit isoform, Cka1 or Cka2, suffices, but previous genetic evidence suggests that the isoforms have some distinct roles. In this work, we present evidence that the transcriptional repressor Nrg1, which regulates various stress-responsive genes, is a downstream target of CK2 containing the Cka1 isoform. We found that Nrg1 is phosphorylated in response to stress and that its phosphorylation was defective in cka1Delta, but not cka2Delta, mutants. Thus, the Cka1 catalytic subunit isoform is specifically required for phosphorylation of Nrg1 in vivo. The CK2 regulatory subunits were also required, indicating that the CK2 holoenzyme is involved. Both yeast and recombinant human CK2 phosphorylated recombinant Nrg1 in vitro. This identification of a protein whose phosphorylation requires a specific CK2 catalytic subunit isoform supports the view that the two isoforms exhibit functional specificity in vivo.
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