Date of Award
2008
Publication Type
Master Thesis
Degree Name
M.Sc.
Department
Chemistry and Biochemistry
Keywords
Biochemistry, General.
Supervisor
Vacratsis, Panayiotis (Chemistry & Biochemistry)
Rights
info:eu-repo/semantics/openAccess
Creative Commons License
This work is licensed under a Creative Commons Attribution-NonCommercial-No Derivative Works 4.0 International License.
Abstract
YVH1 (DUSP12) is a highly conserved atypical dual-specificity phosphatase. Yeast deletion studies have suggested YVH1 plays a role in cell growth. However, the physiological role of the human orthologue is unknown. Our lab has determined that hYVH1 interacts with HSP70, a heat shock protein that plays a cell survival role. The focus of this study was to further characterize this interaction, and attempt to determine its functional significance. Results determined that this interaction is mediated through the ATPase domain of HSP70 and requires the zinc binding domain of hYVH1. Moreover, hYVH1 was found to be uncompetitively inhibited by ATP. Functional examination determined that catalytic activity of each enzyme is not affected by this interaction. Evidence suggests that over-expression of hYVH1 alters the localization of HSP70 during heat stress. Therefore, our results suggest that the HSP70-hYVH1 interaction may be critical for positioning these cell survival proteins during times of cellular stress.
Recommended Citation
Mucaki, Eliseos John, "Functional characterization of the interaction between heat shock protein 70 and the human dual-specificity phosphatase YVH1" (2008). Electronic Theses and Dissertations. 2171.
https://scholar.uwindsor.ca/etd/2171