Protein kinase CK2 Copper Drosophila CK2 Molecular Biology
Casein kinase 2 (CK2) is a an evolutionarily conserved, heterotetrameric serine/threonine kinase involved in a wide range of diverse cellular functions from transcription to regulation of the cell cycle to control of circadian rhythms. Not surprisingly, dysregulation of this kinase has been observed in multiple disease states, particularly 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 identified to date. However, most peculiar is the apparent constitutive activity of this enzyme: no definitive mode of regulation has thus far been identified. Toward this end, we have recently discovered that the transition metal copper binds directly to CK2 and enhances the catalytic activity of the kinase both in vitro and in mammalian cell-based assays. Here, using genetic approaches in D. melanogaster, we extend these findings and demonstrate that copper also functions as a key modulator of CK2 kinase activity in the fly. Taken together, our data suggest that copper is a critical regulator of CK2 and CK2-mediated signaling pathways both in vitro and in vivo.
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Details
Title
Exploring the copper mediated regulation of casein kinase 2 in D. melanogaster
Creators
Sarah Stewart Nicolson
Contributors
Todd Strochlic (Advisor)
Awarding Institution
Drexel University
Degree Awarded
Master of Science (M.S.)
Publisher
Drexel University; Philadelphia, Pennsylvania
Number of pages
v, 24 pages
Resource Type
Thesis
Language
English
Academic Unit
Biochemistry and Molecular Biology; College of Medicine; Drexel University
Other Identifier
991019104611304721
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