NDLI: Melatonin and ubiquitin: what’s the connection?

Content Provider	Springer Nature Link
Author	Vriend, Jerry Reiter, Russel J.
Copyright Year	2014
Abstract	Melatonin has been widely studied for its role in photoperiodism in seasonal breeders; it is also a potent antioxidant. Ubiquitin, a protein also widespread in living cells, contributes to many cellular events, although the most well known is that of tagging proteins for destruction by the proteasome. Herein, we suggest a model in which melatonin interacts with the ubiquitin–proteasome system to regulate a variety of seemingly unrelated processes. Ubiquitin, for example, is a major regulator of central activity of thyroid hormone type 2 deiodinase; the subsequent regulation of T3 may be central to the melatonin-induced changes in seasonal reproduction and seasonal changes in metabolism. Both melatonin and ubiquitin also have important roles in protecting cells from oxidative stress. We discuss the interaction of melatonin and the ubiquitin–proteasome system in oxidative stress through regulation of the ubiquitin-activating enzyme, E1. Previous reports have shown that glutathiolation of this enzyme protects proteins from unnecessary degradation. In addition, evidence is discussed concerning the interaction of ubiquitin and melatonin in activation of the transcription factor NF-κB as well as modulating cellular levels of numerous signal transducing factors including the tumor suppressor, p53. Some of the actions of melatonin on the regulatory particle of the proteasome appear to be related to its inhibition of the calcium-dependent calmodulin kinase II, an enzyme which reportedly copurifies with proteasomes. Many of the actions of melatonin on signal transduction are similar to those of a proteasome inhibitor. While these actions of melatonin could be explained by a direct inhibitory action on the catalytic core particle of the proteasome, this has not been experimentally verified. If our hypothesis of melatonin as a general inhibitor of the ubiquitin–proteasome system is confirmed, it is predicted that more examples of this interaction will be demonstrated in a variety of tissues in which ubiquitin and melatonin co-exist. Furthermore, the hypothesis of melatonin as an inhibitor of the ubiquitin–proteasome system will be a very useful model for clinical testing of melatonin.
Starting Page	3409
Ending Page	3418
Page Count	10
File Format	PDF
ISSN	1420682X
Journal	Cellular and Molecular Life Sciences
Volume Number	71
Issue Number	18
e-ISSN	14209071
Language	English
Publisher	Springer Basel
Publisher Date	2014-06-12
Publisher Place	Basel
Access Restriction	Subscribed
Subject Keyword	Ubiquitination Transcription factor Signal transduction VEGF AKT Protein degradation Mitochondria Calmodulin Cell Biology Biomedicine general Life Sciences Biochemistry
Content Type	Text
Resource Type	Article
Subject	Cell Biology Molecular Biology Molecular Medicine Pharmacology Cellular and Molecular Neuroscience

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