G Protein-Coupled Receptors in the Sweet Spot: Glycosylation and other Post-translational Modifications

Research output: Contribution to journal › Review › Research › peer-review

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G Protein-Coupled Receptors in the Sweet Spot : Glycosylation and other Post-translational Modifications. / Goth, Christoffer K.; Petaja-Repo, Ulla E.; Rosenkilde, Mette M.

In: ACS Pharmacology & Translational Science, Vol. 3, No. 2, 2020, p. 237-245.

Research output: Contribution to journal › Review › Research › peer-review

Harvard

Goth, CK, Petaja-Repo, UE & Rosenkilde, MM 2020, 'G Protein-Coupled Receptors in the Sweet Spot: Glycosylation and other Post-translational Modifications', ACS Pharmacology & Translational Science, vol. 3, no. 2, pp. 237-245. https://doi.org/10.1021/acsptsci.0c00016

APA

Goth, C. K., Petaja-Repo, U. E., & Rosenkilde, M. M. (2020). G Protein-Coupled Receptors in the Sweet Spot: Glycosylation and other Post-translational Modifications. ACS Pharmacology & Translational Science, 3(2), 237-245. https://doi.org/10.1021/acsptsci.0c00016

Vancouver

Goth CK, Petaja-Repo UE, Rosenkilde MM. G Protein-Coupled Receptors in the Sweet Spot: Glycosylation and other Post-translational Modifications. ACS Pharmacology & Translational Science. 2020;3(2):237-245. https://doi.org/10.1021/acsptsci.0c00016

Author

Goth, Christoffer K. ; Petaja-Repo, Ulla E. ; Rosenkilde, Mette M. / G Protein-Coupled Receptors in the Sweet Spot : Glycosylation and other Post-translational Modifications. In: ACS Pharmacology & Translational Science. 2020 ; Vol. 3, No. 2. pp. 237-245.

Bibtex

@article{4a32d45db0704375b1598d213be823ec,
title = "G Protein-Coupled Receptors in the Sweet Spot: Glycosylation and other Post-translational Modifications",
abstract = "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.",
keywords = "glycosylation, tyrosine sulfation, proteolytic cleavage, G protein-coupled receptor, PTM interplay, N-LINKED GLYCOSYLATION, CELL-SURFACE EXPRESSION, EXTRACELLULAR LOOP 2, O-GLYCOSYLATION, BETA(1)-ADRENERGIC RECEPTOR, ACTIVATED RECEPTOR-1, TYROSINE SULFATION, QUALITY-CONTROL, HUMAN CYTOMEGALOVIRUS, DISULFIDE BRIDGES",
author = "Goth, {Christoffer K.} and Petaja-Repo, {Ulla E.} and Rosenkilde, {Mette M.}",
year = "2020",
doi = "10.1021/acsptsci.0c00016",
language = "English",
volume = "3",
pages = "237--245",
journal = "ACS Pharmacology and Translational Science",
issn = "2575-9108",
publisher = "ACS Publications",
number = "2",

}

RIS

TY - JOUR

T1 - G Protein-Coupled Receptors in the Sweet Spot

T2 - Glycosylation and other Post-translational Modifications

AU - Goth, Christoffer K.

AU - Petaja-Repo, Ulla E.

AU - Rosenkilde, Mette M.

PY - 2020

Y1 - 2020

N2 - 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.

AB - 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.

KW - glycosylation

KW - tyrosine sulfation

KW - proteolytic cleavage

KW - G protein-coupled receptor

KW - PTM interplay

KW - N-LINKED GLYCOSYLATION

KW - CELL-SURFACE EXPRESSION

KW - EXTRACELLULAR LOOP 2

KW - O-GLYCOSYLATION

KW - BETA(1)-ADRENERGIC RECEPTOR

KW - ACTIVATED RECEPTOR-1

KW - TYROSINE SULFATION

KW - QUALITY-CONTROL

KW - HUMAN CYTOMEGALOVIRUS

KW - DISULFIDE BRIDGES

U2 - 10.1021/acsptsci.0c00016

DO - 10.1021/acsptsci.0c00016

M3 - Review

C2 - 32296765

VL - 3

SP - 237

EP - 245

JO - ACS Pharmacology and Translational Science

JF - ACS Pharmacology and Translational Science

SN - 2575-9108

IS - 2

ER -

ID: 256891020