ArticleMolecular and cellular biochemistry2001
Identification and characterization of proteins that interact with Drosophila melanogaster protein kinase CK2.
Article in Molecular and cellular biochemistry, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 17 citations in OpenAlex.
- Casein kinase 2 phosphorylates and induces the SALL2 tumor suppressor degradation in colon cancer cells.Cell death & disease · 2024Article
- Protein kinase CK2 phosphorylates a conserved motif in the Notch effector E(spl)-Mγ.Molecular and cellular biochemistry · 2023Article
- Drosophila Protein Kinase CK2: Genetics, Regulatory Complexity and Emerging Roles during Development.Pharmaceuticals (Basel, Switzerland) · 2016Review
- Control of Neural Daughter Cell Proliferation by Multi-level Notch/Su(H)/E(spl)-HLH Signaling.PLoS genetics · 2016Article
- Phosphorylation of TGB1 by protein kinase CK2 promotes barley stripe mosaic virus movement in monocots and dicots.Journal of experimental botany · 2015Article
- 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
- The nucleolar protein SURF-6 is essential for viability in mouse NIH/3T3 cells.Molecular biology reports · 2007Article
- Drosophila CK2 phosphorylates Deadpan, a member of the HES family of basic-helix-loop-helix (bHLH) repressors.Molecular and cellular biochemistry · 2005Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
D. melanogaster CK2 (DmCK2) is a highly conserved protein kinase that is composed of catalytic, alpha, and regulatory, beta, subunits associated as an alpha2beta2 heterotetramer. In order to analyze the functions of CK2 in this metazoan model, we have used the two hybrid approach to identify interacting proteins. One of these cDNAs, DmA24, encodes a novel polypeptide with no homologs in GenBank, and is notable in that it contains a bipartite nuclear localization signal and two sites for phosphorylation by CK2. In situ hybridization to polytene chromosomes indicates that the DmA24 gene is located at the 61 D interval of chromosome II a region that also harbors 3 additional genes with similar structure. DmA24p interacts with DmCK2alpha, but not with DmCK2beta, demonstrating that this interaction is specific for the catalytic subunit of CK2. In addition, the protein is phosphorylated by the holoenzyme purified from Drosophila embryos. These studies identify DmA24p as a potentially new physiological partner of DmCK2. In addition, we also report the results of a large-scale screen that has identified a new set of DmCK2-interacting proteins. Most notable among these are Surf6, a nucleolar protein involved in RNA processing, and Spalt, a homeotic protein.
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