Phosphomimetic Mutation of the N-Terminal Lid of MDM2 Enhances the Polyubiquitination of p53 through Stimulation of E2-Ubiquitin Thioester Hydrolysis
Journal Article
Fraser, J. A., Worrall, E. G., Lin, Y., Landre, V., Pettersson, S., Blackburn, E., …Hupp, T. R. (2015)
Phosphomimetic Mutation of the N-Terminal Lid of MDM2 Enhances the Polyubiquitination of p53 through Stimulation of E2-Ubiquitin Thioester Hydrolysis. Journal of Molecular Biology, 427(8), 1728-1747. https://doi.org/10.1016/j.jmb.2014.12.011
Mouse double minute 2 (MDM2) has a phosphorylation site within a lid motif at Ser17 whose phosphomimetic
mutation to Asp17 stimulates MDM2-mediated polyubiquitination of p53. ...
The MDM2 Ubiquitination Signal in the DNA-Binding Domain of p53 Forms a Docking Site for Calcium Calmodulin Kinase Superfamily Members
Journal Article
Craig, A. L., Chrystal, J. A., Fraser, J. A., Sphyris, N., Lin, Y., Harrison, B. J., …Hupp, T. R. (2007)
The MDM2 Ubiquitination Signal in the DNA-Binding Domain of p53 Forms a Docking Site for Calcium Calmodulin Kinase Superfamily Members. Molecular and Cellular Biology, 27(9), 3542-3555. https://doi.org/10.1128/mcb.01595-06
Genetic and biochemical studies have shown that Ser20 phosphorylation in the transactivation domain of p53 mediates p300-catalyzed DNA-dependent p53 acetylation and B-cell tum...
The Modifier Subunit of Drosophila Glutamate-Cysteine Ligase Regulates Catalytic Activity by Covalent and Noncovalent Interactions and Influences Glutathione Homeostasis in Vivo
Journal Article
Fraser, J. A., Kansagra, P., Kotecki, C., Saunders, R. D. C., & McLellan, L. I. (2003)
The Modifier Subunit of Drosophila Glutamate-Cysteine Ligase Regulates Catalytic Activity by Covalent and Noncovalent Interactions and Influences Glutathione Homeostasis in Vivo. Journal of Biological Chemistry, 278(47), 46369-46377. https://doi.org/10.1074/jbc.m308035200
Glutamate-cysteine ligase (GCL) has a key influence on glutathione homeostasis. It has been proposed that mammalian GCL is regulated by the redox environment, and we show here...