Tseng, W-Y, Stacey, M orcid.org/0000-0003-3502-5542 and Lin, H-H (Cover date: March 2 2023) Role of Adhesion G Protein-Coupled Receptors in Immune Dysfunction and Disorder. International Journal of Molecular Sciences, 24 (6). 5499. ISSN 1661-6596
Abstract
Adhesion G protein-coupled receptors (aGPCRs) make up the second-largest GPCR subfamily which comprises a total of 33 different members in humans [1]. Several distinctive structural and functional characteristics of aGPCRs set them apart from other GPCRs. The N-terminal extracellular region of aGPCRs is markedly large and comprises many different cell-adhesive protein motifs arranged in tandem or in mixed combination. These protein motifs, including the epidermal growth factor (EGF)-, immunoglobulin (Ig)-, lectin-, leucine-rich repeat (LRR)-, pentraxin (PTX)-, thrombospondin (TSP)-like, and hormone-binding domains, all have well-known protein–protein interaction and cellular adhesion functions. A hallmark GPCR autoproteolysis-inducing (GAIN) domain is located immediately after the cell-adhesive protein motifs and before the signature seven-transmembrane (7TM) domain (Figure 1). These structural features stipulate bilateral extracellular adhesion and intracellular signaling functions for aGPCRs. Indeed, diverse ligands/interacting partners of endogenous and exogenous origins, including soluble, cell surface, and cell matrix proteins, carbohydrates, lipids, and microbial products have been identified for aGPCRs. In addition, both G protein-dependent and -independent signaling pathways were known to be induced by aGPCRs.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | © 2023 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
Keywords: | adhesion GPCRs; immune dysfunction; immune disorder; ligand; signaling |
Dates: |
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Institution: | The University of Leeds |
Academic Units: | The University of Leeds > Faculty of Biological Sciences (Leeds) > School of Molecular and Cellular Biology (Leeds) |
Depositing User: | Symplectic Publications |
Date Deposited: | 23 May 2023 14:03 |
Last Modified: | 23 May 2023 14:12 |
Status: | Published |
Publisher: | MDPI |
Identification Number: | 10.3390/ijms24065499 |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:199477 |
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