ArticleMolecular and cellular biochemistry2009
Drosophila protein kinase CK2 is rendered temperature-sensitive by mutations of highly conserved residues flanking the activation segment.
Article in Molecular and cellular biochemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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Who cites it
9 citing papers in PubMed, 14 citations in OpenAlex.
- Synthetic biology approaches to generate temperature-sensitive alleles for the Sterile Insect Technique.Insect science · 2026Review
- Review
- Identification of de novo CSNK2A1 and CSNK2B variants in cases of global developmental delay with seizures.Journal of human genetics · 2019Article
- Protein Kinase CK2: Intricate Relationships within Regulatory Cellular Networks.Pharmaceuticals (Basel, Switzerland) · 2017Review
- Drosophila Protein Kinase CK2: Genetics, Regulatory Complexity and Emerging Roles during Development.Pharmaceuticals (Basel, Switzerland) · 2016Review
- GSK-3 and CK2 Kinases Converge on Timeless to Regulate the Master Clock.Cell reports · 2016Article
- PINK1 rendered temperature sensitive by disease-associated and engineered mutations.Human molecular genetics · 2013Article
- New insights into the Orange domain of E(spl)-M8, and the roles of the C-terminal domain in autoinhibition and Groucho recruitment.Molecular and cellular biochemistry · 2011Article
- Functional dissection of Timekeeper (Tik) implicates opposite roles for CK2 and PP2A during Drosophila neurogenesis.Genesis (New York, N.Y. : 2000) · 2009Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
CK2 is a Ser/Thr protein kinase essential for animal development. Although null alleles for CK2 are available in the mouse and Drosophila models, they are lethal when homozygous, thus necessitating conditional alleles for analysis of its developmental roles. We describe the isolation of temperature-sensitive (ts) alleles of Drosophila CK2alpha (dCK2alpha). These alleles efficiently rescue lethality of yeast lacking endogenous CK2 at 29 degrees C, but this ability is lost at higher temperatures in an allele-specific manner. These ts-variants exhibit properties akin to the wild type protein, and interact robustly with dCK2beta. Modeling of these ts-variants using the crystal structure of human CK2alpha indicates that the affected residues are in close proximity to the active site. We find that substitution of Asp(212) elicits potent ts-behavior, an important finding because this residue contributes to stability of the activation segment and is invariant in other Ser/Thr protein kinases.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.