Semester
Fall
Date of Graduation
2005
Document Type
Thesis
Degree Type
MS
College
Eberly College of Arts and Sciences
Department
Biology
Committee Chair
Clifton Bishop
Abstract
Protein kinase CK2 is a serine/threonine protein kinase ubiquitously expressed in eukaryotic organisms. The enzyme is composed of 2 alpha (catalytic) subunits and 2 beta (regulatory) subunits. The minimum consensus site for CK2 phosphorylation is S/TXXD/E, where "X" is any non-basic amino acid. Substrates so far identified include proteins associated with cell cycle regulation and development.;In Drosophila melanogaster, the Notch pathway activates members of the Enhancer-of-split Complex [E(spl)-C]. m8, which is a member of the E(spl)-C, was found to interact with and be phosphorylated by CK2. The physiological affects of CK2 phosphorylation were studied in vivo through the Gal4-UAS system. Flies with a reduced eye phenotype were identified in a cross between scaGal4 and the transgenic line m8S 159D. Two-hybrid analysis indicated m8S159D interacted significantly stronger with the proneural bHLH protein Atonal than either m8 or m8S159A. These results are the first indication that phosphorylation plays a role in the regulation of E(spl)-C proteins and also the first implication of a role for CK2 during neurogenesis.
Recommended Citation
Trott, Regina L., "Drosophila melanogaster protein kinase CK2 interacts with and phosphorylates the neurogenic repressor m8 resulting in the production of a novel eye phenotype" (2005). Graduate Theses, Dissertations, and Problem Reports. 4201.
https://researchrepository.wvu.edu/etd/4201
