Biological characterization of hYVH1
Date of Award
Chemistry and Biochemistry
Creative Commons License
This work is licensed under a Creative Commons Attribution-Noncommercial-No Derivative Works 4.0 License.
Human YVH1 is an atypical dual specificity phosphatase (DSP) that is widely conserved throughout evolution. Deletion studies in yeast have suggested a role for this phosphatase in regulating cell growth, sporulation, and glycogen accumulation. However, the functional role of the human orthologue is unknown. This study examines the interaction between hYVH1 and a recently identified binding partner Hsp70, in addition to deciphering domains and motifs important in hYVH1 localization. The results established that the zinc binding domain mediates the subcellular targeting of hYVH1. Moreover, a putative nuclear export sequence was identified to have some effect on the shuttling of hYVH1 between the nucleus and cytoplasm. Hsp70 and hYVH1 were found to be colocalized to the perinuclear region following heat stress. Furthermore, hYVH1 expression repressed heat shock induced cell death. The results suggest that hYVH1 cooperates with Hsp70 to positively affect cell viability by targeting the MAPK signaling pathway.
Sharda, Priya, "Biological characterization of hYVH1" (2007). Electronic Theses and Dissertations. 4626.