Title:

Characterization of the Role of Ubiquitin Protein Ligase E3 Component N-recognin 4 (UBR4) in the Murine Circadian Clock

Author: Ling, Harrod
Issue Date: Nov-2014
Abstract (summary): Ubiquitination is an important post-translational modification in the molecular clock that regulates degradation of clock proteins through ubiquitin ligases. However, no ubiquitin ligase has been implicated in the photic entrainment pathways in mammals thus far. In this thesis, I characterized the physiological and molecular phenotype of a new ubiquitin ligase named UBR4 in the murine circadian clock. UBR4 is expressed throughout the suprachiasmatic nucleus in a time-of-day-dependent fashion and is light-inducible in the early subjective night. Homozygous ubr4 knockout are embryonic lethal, therefore heterozygous ubr4 mice (ubr4+/-) were used to study its physiological role in the circadian clock. I found that mice with reduced expression of UBR4 show differential phenotype in circadian paradigms that involve chronic light disturbances. Furthermore, preliminary data suggest that casein kinase 2 beta subunit is a potential substrate of UBR4, affecting molecular clock component PER in vivo and in vitro.
Content Type: Thesis

Permanent link

https://hdl.handle.net/1807/68000

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