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Deciphering The Ck2-Dependent Phosphoproteome And Its Integration With Regulatory Ptm Networks, Teresa Nunez De Villavicencio Diaz
Deciphering The Ck2-Dependent Phosphoproteome And Its Integration With Regulatory Ptm Networks, Teresa Nunez De Villavicencio Diaz
Electronic Thesis and Dissertation Repository
Protein functions are regulated by the post-translational addition of covalent modifications on certain amino acids. Depending on their distance within the 3-dimensional structure, addition/removal of individual post translational modifications (PTMs) can be impacted by others. This PTM interplay constitutes an essential regulatory mechanism that interconnects the molecular networks in the cell. Protein CK2, a clinically relevant acidophilic Ser/Thr kinase, may be responsible for 10-20% of the human phosphoproteome. Such estimates agree with the number of known substrates, which continues to expand. Furthermore, the demonstration that CK2 participates in hierarchical phosphorylation and has similar sequence determinants to caspases suggest extensive PTM …
Quinone Reductase 2 Roles In Proteomic Regulation And Response To Treatment With Clinical Drugs, Matthew D. Walker
Quinone Reductase 2 Roles In Proteomic Regulation And Response To Treatment With Clinical Drugs, Matthew D. Walker
Electronic Thesis and Dissertation Repository
Detoxification of quinone compounds is catalyzed by the NQO1 protein in humans. The related NQO2 is distinct from NQO1 as it uses NRH preferentially as a co-substrate to the exclusion of NAD(P)H. It is uncertain if NRH is available in cells for use by NQO2 and raises doubts that quinone detoxification is the adaptive role for NQO2. This study employed cell biology, protein structure and proteomics approaches to identify functions for NQO2 relevant to a cellular context. Several NQO2 interacting clinical drugs were found to have cytotoxic effects dependent upon NQO2 expression. Results from proteomic experiments identified novel roles for …