ArticlePharmaceuticals (Basel, Switzerland)2016
The Phosphorylation of PDX-1 by Protein Kinase CK2 Is Crucial for Its Stability.
Article in Pharmaceuticals (Basel, Switzerland), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Article
- CK2 activity is crucial for proper glucagon expression.Diabetologia · 2024Article
- PCIF1, the only methyltransferase of N6,2-O-dimethyladenosine.Cancer cell international · 2023Review
- Phosphorylation of Thymidylate Synthase and Dihydrofolate Reductase in Cancer Cells and the Effect of CK2α Silencing.International journal of molecular sciences · 2023Article
- SGC-CK2-1 Is an Efficient Inducer of Insulin Production and Secretion in Pancreatic β-Cells.Pharmaceutics · 2021Article
- CK2 Regulation: Perspectives in 2021.Biomedicines · 2021Review
- Protein Kinase CK2 Controls CaInternational journal of molecular sciences · 2020Article
- Protein Kinase CK2-A Putative Target for the Therapy of Diabetes Mellitus?International journal of molecular sciences · 2019Review
- Functional interplay between the transcription factors USF1 and PDX-1 and protein kinase CK2 in pancreatic β-cells.Scientific reports · 2017Article
- An Updated View on an Emerging Target: Selected Papers from the 8th International Conference on Protein Kinase CK2.Pharmaceuticals (Basel, Switzerland) · 2017Article
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Authors and funding
4 authors.
Funding
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Abstract
The homeodomain protein PDX-1 is a critical regulator of pancreatic development and insulin production in pancreatic β-cells. We have recently shown that PDX-1 is a substrate of protein kinase CK2; a multifunctional protein kinase which is implicated in the regulation of various cellular aspects, such as differentiation, proliferation, and survival. The CK2 phosphorylation site of PDX-1 is located within the binding region of the E3 ubiquitin ligase adaptor protein PCIF1. To study the interaction between PDX-1 and PCIF1 we used immunofluorescence analysis, co-immunoprecipitation, GST-pull-down studies, and proximity ligation assay (PLA). For the analysis of the stability of PDX-1 we performed a cycloheximide chase. We used PDX-1 in its wild-type form as well as phosphomutants of the CK2 phosphorylation site. In pancreatic β-cells PDX-1 binds to PCIF1. The phosphorylation of PDX-1 by CK2 increases the ratio of PCIF1 bound to PDX-1. The stability of PDX-1 is extended in the absence of CK2 phosphorylation. Our results identified protein kinase CK2 as new important modulator of the stability of PDX-1.
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