Osama Abdalla

Death of a Protein by Osama Abdalla & Brittany Mascarenhas (Cheng Lab)

The Department of Biology is proud to feature the latest paper from Cheng Lab, authored by Osama Abdalla & Brittany Mascarenhas, from Cheng Lab, and published by the International Journal of Molecular Sciences:

Death of a Protein: The Role of E3 Ubiquitin Ligases in Circadian Rhythms of Mice and Flies

https://doi.org/10.3390/ijms231810569

Circadian clocks evolved to enable organisms to anticipate and prepare for periodic environmental

Brittany Mascarenhas
Brittany Mascarenhas

changes driven by the day–night cycle. This internal timekeeping mechanism is built on autoregulatory transcription–translation feedback loops that control the rhythmic expression of core clock genes and their protein products. The levels of clock proteins rise and ebb throughout a 24-h period through their rhythmic synthesis and destruction. In the ubiquitin–proteasome system, the process of polyubiquitination, or the covalent attachment of a ubiquitin chain, marks a protein for degradation by the 26S proteasome. The process is regulated by E3 ubiquitin ligases, which recognize specific substrates for ubiquitination. In this review, we summarize the roles that known E3 ubiquitin ligases play in the circadian clocks of two popular model organisms: mice and fruit flies. We also discuss emerging evidence that implicates the N-degron pathway, an alternative proteolytic system, in the regulation of circadian rhythms. We conclude the review with our perspectives on the potential for the proteolytic and non-proteolytic functions of E3 ubiquitin ligases within the circadian clock system.

 

Osama paper pic

 

 

 

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