ArticleThe Biochemical journal2010
Cystic fibrosis transmembrane regulator fragments with the Phe508 deletion exert a dual allosteric control over the master kinase CK2.
Article in The Biochemical journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
What it found
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Who cites it
12 citing papers in PubMed, 24 citations in OpenAlex.
- Protein kinase CK2 and ion channels (Review).Biomedical reports · 2020Review
- NM23 proteins: innocent bystanders or local energy boosters for CFTR?Laboratory investigation; a journal of technical methods and pathology · 2018Review
- The importance of negative determinants as modulators of CK2 targeting. The lesson of Akt2 S131.PloS one · 2018Article
- Strategies for the etiological therapy of cystic fibrosis.Cell death and differentiation · 2017Review
- The Development of CK2 Inhibitors: From Traditional Pharmacology to in Silico Rational Drug Design.Pharmaceuticals (Basel, Switzerland) · 2017Review
- Regulatory Crosstalk by Protein Kinases on CFTR Trafficking and Activity.Frontiers in chemistry · 2016Review
- A "SYDE" effect of hierarchical phosphorylation: possible relevance to the cystic fibrosis basic defect.Cellular and molecular life sciences : CMLS · 2014Article
- CFTR mutations altering CFTR fragmentation.The Biochemical journal · 2013Article
- Casein kinase 2α regulates multidrug resistance-associated protein 1 function via phosphorylation of Thr249.Molecular pharmacology · 2012Article
- Contribution of casein kinase 2 and spleen tyrosine kinase to CFTR trafficking and protein kinase A-induced activity.Molecular and cellular biology · 2011Article
- Understanding protein kinase CK2 mis-regulation upon F508del CFTR expression.Naunyn-Schmiedeberg's archives of pharmacology · 2011Review
- Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
Cystic fibrosis mostly follows a single Phe508 deletion in CFTR (cystic fibrosis transmembrane regulator) (CFTRDeltaF508), thereby causing premature fragmentation of the nascent protein with concomitant alterations of diverse cellular functions. We show that CK2, the most pleiotropic protein kinase, undergoes allosteric control of its different cellular forms in the presence of short CFTR peptides encompassing the Phe508 deletion: these CFTRDeltaF508 peptides drastically inhibit the isolated catalytic subunit (alpha) of the kinase and yet up-regulate the holoenzyme, composed of two catalytic and two non-catalytic (beta) subunits. Remarkable agreement between in silico docking and our biochemical data point to different sites for the CFTRDeltaF508 peptide binding on isolated CK2alpha and on CK2beta assembled into the holoenzyme, suggesting that CK2 targeting may be perturbed in cells expressing CFTRDeltaF508; this could shed light on some pleiotropic aspects of cystic fibrosis disease.
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Registered trials
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