Review
Version 1
Preserved in Portico This version is not peer-reviewed
Regulation of G Protein-Coupled Receptors by Ubiquitination
Version 1
: Received: 20 April 2017 / Approved: 21 April 2017 / Online: 21 April 2017 (06:23:26 CEST)
A peer-reviewed article of this Preprint also exists.
Skieterska, K.; Rondou, P.; Van Craenenbroeck, K. Regulation of G Protein-Coupled Receptors by Ubiquitination. Int. J. Mol. Sci. 2017, 18, 923. Skieterska, K.; Rondou, P.; Van Craenenbroeck, K. Regulation of G Protein-Coupled Receptors by Ubiquitination. Int. J. Mol. Sci. 2017, 18, 923.
Abstract
G protein-coupled receptors (GPCRs) comprise the largest family of membrane receptors that control many cellular processes and consequently often serve as drug targets. These receptors undergo a strict regulation by mechanisms such as internalization and desensitization, which are strongly influenced by posttranslational modifications. Ubiquitination is a posttranslational modification with a broad range of functions that is currently gaining increased appreciation as a regulator of GPCR activity. The role of ubiquitination in directing GPCRs for lysosomal degradation has already been well-established. Furthermore, this modification can also play a role in targeting membrane and endoplasmic reticulum-associated receptors to the proteasome. Most recently, ubiquitination was also shown to be involved in GPCR signaling. In this review, we present current knowledge on the molecular basis of GPCR regulation by ubiquitination, and highlight the importance of E3 ubiquitin ligases, deubiquitinating enzymes and β-arrestins. Finally, we discuss classical and newly-discovered functions of ubiquitination in controlling GPCR activity.
Keywords
GPCR; ubiquitination; β-arrestin; deubiquitinating enzyme; E3 ubiquitin ligase
Subject
Biology and Life Sciences, Biochemistry and Molecular Biology
Copyright: This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
Comments (0)
We encourage comments and feedback from a broad range of readers. See criteria for comments and our Diversity statement.
Leave a public commentSend a private comment to the author(s)
* All users must log in before leaving a comment