University of Oulu

Goth, Christoffer K.; Petäjä-Repo, Ulla E.; Rosenkilde, Mette M.; G protein-coupled receptors in the sweet spot : glycosylation and other post-translational modifications; ACS Pharmacol. Transl. Sci. 2020, 3, 2, 237-245.

G protein-coupled receptors in the sweet spot : glycosylation and other post-translational modifications

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Author: Goth, Christoffer K.1; Petäjä-Repo, Ulla E.2; Rosenkilde, Mette M.1
Organizations: 1Laboratory for Molecular Pharmacology, Department of Biomedical Sciences, Faculty of Health and Medical Sciences, University of Copenhagen, Copenhagen, DK 2200, Denmark
2Medical Research Center Oulu, Research Unit of Biomedicine, University of Oulu, Oulu, FI-90014, Finland
Format: article
Version: accepted version
Access: open
Online Access: PDF Full Text (PDF, 1.6 MB)
Persistent link:
Language: English
Published: American Chemical Society, 2020
Publish Date: 2021-03-17


Post-translational modifications (PTMs) are a fundamental phenomenon across all classes of life and several hundred different types have been identified. PTMs contribute widely to the biological functions of proteins and greatly increase their diversity. One important class of proteins regulated by PTMs, is the cell surface expressed G protein-coupled receptors (GPCRs). While most PTMs have been shown to exert distinct biological functions, we are only beginning to approach the complexity that the potential interplay between different PTMs may have on biological functions and their regulation. Importantly, PTMs and their potential interplay represent an appealing mechanism for cell and tissue specific regulation of GPCR function and may partially contribute to functional selectivity of some GPCRs. In this review we highlight examples of PTMs located in GPCR extracellular domains, with special focus on glycosylation and the potential interplay with other close-by PTMs such as tyrosine sulfation, proteolytic cleavage, and phosphorylation.

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Series: ACS pharmacology & translational science
ISSN: 2575-9108
ISSN-E: 2575-9108
ISSN-L: 2575-9108
Volume: 3
Issue: 2
Pages: 237 - 245
DOI: 10.1021/acsptsci.0c00016
Type of Publication: A2 Review article in a scientific journal
Field of Science: 3111 Biomedicine
Funding: This work was funded by the Academy of Finland, European Research Council (VIREX Grant agreement 682549, CallERC-2105-CoG), The Lundbeck Foundation (large project grant - R242-2017-409), and the Novo Nordisk Foundation (NNF17OC0029222).
Copyright information: This document is the Accepted Manuscript version of a Published Work that appeared in final form in ACS Pharmacol. Transl. Sci., copyright © American Chemical Society after peer review and technical editing by the publisher. To access the final edited and published work see [insert ACS Articles on Request author-directed link to Published Work, see