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Journal article
Copper Modulates the Catalytic Activity of Protein Kinase CK2
Frontiers in molecular biosciences, v 9, pp 878652-878652
09 Jun 2022
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
Casein kinase 2 (CK2) is an evolutionarily conserved serine/threonine kinase implicated in a wide range of cellular functions and known to be dysregulated in various diseases such as cancer. Compared to most other kinases, CK2 exhibits several unusual properties, including dual co-substrate specificity and a high degree of promiscuity with hundreds of substrates described to date. Most paradoxical, however, is its apparent constitutive activity: no definitive mode of catalytic regulation has thus far been identified. Here we demonstrate that copper enhances the enzymatic activity of CK2 both in vitro and in vivo . We show that copper binds directly to CK2, and we identify specific residues in the catalytic subunit of the enzyme that are critical for copper-binding. We further demonstrate that increased levels of intracellular copper result in enhanced CK2 kinase activity, while decreased copper import results in reduced CK2 activity. Taken together, these findings establish CK2 as a copper-regulated kinase and indicate that copper is a key modulator of CK2-dependent signaling pathways.
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Details
- Title
- Copper Modulates the Catalytic Activity of Protein Kinase CK2
- Creators
- John E. Chojnowski - Drexel UniversityRongrong LiTiffany TsangFatimah H. AlfaranAlexej DickSimon CocklinDonita C. BradyTodd I. Strochlic
- Publication Details
- Frontiers in molecular biosciences, v 9, pp 878652-878652
- Publisher
- Frontiers
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Biochemistry and Molecular Biology
- Web of Science ID
- WOS:000815001600001
- Scopus ID
- 2-s2.0-85133416852
- Other Identifier
- 991019168789604721
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- Collaboration types
- Domestic collaboration
- Web of Science research areas
- Biochemistry & Molecular Biology