Dissecting signaling and functions of adhesion G protein-coupled receptors

Demet Araç; Gabriela Aust; Davide Calebiro; Felix B Engel; Caroline Formstone; André Goffinet; Jörg Hamann; Robert J Kittel; Ines Liebscher; Hsi-Hsien Lin; Kelly R Monk; Alexander Petrenko; Xianhua Piao; Simone Prömel; Helgi B Schiöth; Thue W. Schwartz; Martin Stacey; Yuri A Ushkaryov; Manja Wobus; Uwe Wolfrum; Lei Xu; Tobias Langenhan

doi:10.1111/j.1749-6632.2012.06820.x

Dissecting signaling and functions of adhesion G protein-coupled receptors

Demet Araç, Gabriela Aust, Davide Calebiro, Felix B Engel, Caroline Formstone, André Goffinet, Jörg Hamann, Robert J Kittel, Ines Liebscher, Hsi-Hsien Lin, Kelly R Monk, Alexander Petrenko, Xianhua Piao, Simone Prömel, Helgi B Schiöth, Thue W. Schwartz, Martin Stacey, Yuri A Ushkaryov, Manja Wobus, Uwe WolfrumLei Xu, Tobias Langenhan

31 Citations (Scopus)

Abstract

G protein-coupled receptors (GPCRs) comprise an expanded superfamily of receptors in the human genome. Adhesion class G protein-coupled receptors (adhesion-GPCRs) form the second largest class of GPCRs. Despite the abundance, size, molecular structure, and functions in facilitating cell and matrix contacts in a variety of organ systems, adhesion-GPCRs are by far the most poorly understood GPCR class. Adhesion-GPCRs possess a unique molecular structure, with extended N-termini containing various adhesion domains. In addition, many adhesion-GPCRs are autoproteolytically cleaved into an N-terminal fragment (NTF, NT, α-subunit) and C-terminal fragment (CTF, CT, β-subunit) at a conserved GPCR autoproteolysis-inducing (GAIN) domain that contains a GPCR proteolysis site (GPS). These two features distinguish adhesion-GPCRs from other GPCR classes. Though active research on adhesion-GPCRs in diverse areas, such as immunity, neuroscience, and development and tumor biology has been intensified in the recent years, the general biological and pharmacological properties of adhesion-GPCRs are not well known, and they have not yet been used for biomedical purposes. The "6th International Adhesion-GPCR Workshop," held at the Institute of Physiology of the University of Würzburg on September 6-8, 2012, assembled a majority of the investigators currently actively pursuing research on adhesion-GPCRs, including scientists from laboratories in Europe, the United States, and Asia. The meeting featured the nascent mechanistic understanding of the molecular events driving the signal transduction of adhesion-GPCRs, novel models to evaluate their functions, and evidence for their involvement in human disease.

Original language	English
Journal	Annals of the New York Academy of Sciences
Volume	1276
Pages (from-to)	1-25
Number of pages	25
ISSN	0077-8923
DOIs	https://doi.org/10.1111/j.1749-6632.2012.06820.x
Publication status	Published - Dec 2012

Keywords

Cell Adhesion
Humans
Ligands
Models, Biological
Proteolysis
Receptors, G-Protein-Coupled
Signal Transduction

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1111/j.1749-6632.2012.06820.x

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Araç, D., Aust, G., Calebiro, D., Engel, F. B., Formstone, C., Goffinet, A., Hamann, J., Kittel, R. J., Liebscher, I., Lin, H-H., Monk, K. R., Petrenko, A., Piao, X., Prömel, S., Schiöth, H. B., Schwartz, T. W., Stacey, M., Ushkaryov, Y. A., Wobus, M., ... Langenhan, T. (2012). Dissecting signaling and functions of adhesion G protein-coupled receptors. Annals of the New York Academy of Sciences, 1276, 1-25. https://doi.org/10.1111/j.1749-6632.2012.06820.x

Araç, D, Aust, G, Calebiro, D, Engel, FB, Formstone, C, Goffinet, A, Hamann, J, Kittel, RJ, Liebscher, I, Lin, H-H, Monk, KR, Petrenko, A, Piao, X, Prömel, S, Schiöth, HB, Schwartz, TW, Stacey, M, Ushkaryov, YA, Wobus, M, Wolfrum, U, Xu, L & Langenhan, T 2012, 'Dissecting signaling and functions of adhesion G protein-coupled receptors', Annals of the New York Academy of Sciences, vol. 1276, pp. 1-25. https://doi.org/10.1111/j.1749-6632.2012.06820.x

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T1 - Dissecting signaling and functions of adhesion G protein-coupled receptors

AU - Araç, Demet

AU - Aust, Gabriela

AU - Calebiro, Davide

AU - Engel, Felix B

AU - Formstone, Caroline

AU - Goffinet, André

AU - Hamann, Jörg

AU - Kittel, Robert J

AU - Liebscher, Ines

AU - Lin, Hsi-Hsien

AU - Monk, Kelly R

AU - Petrenko, Alexander

AU - Piao, Xianhua

AU - Prömel, Simone

AU - Schiöth, Helgi B

AU - Schwartz, Thue W.

AU - Stacey, Martin

AU - Ushkaryov, Yuri A

AU - Wobus, Manja

AU - Wolfrum, Uwe

AU - Xu, Lei

AU - Langenhan, Tobias

PY - 2012/12

Y1 - 2012/12

N2 - G protein-coupled receptors (GPCRs) comprise an expanded superfamily of receptors in the human genome. Adhesion class G protein-coupled receptors (adhesion-GPCRs) form the second largest class of GPCRs. Despite the abundance, size, molecular structure, and functions in facilitating cell and matrix contacts in a variety of organ systems, adhesion-GPCRs are by far the most poorly understood GPCR class. Adhesion-GPCRs possess a unique molecular structure, with extended N-termini containing various adhesion domains. In addition, many adhesion-GPCRs are autoproteolytically cleaved into an N-terminal fragment (NTF, NT, α-subunit) and C-terminal fragment (CTF, CT, β-subunit) at a conserved GPCR autoproteolysis-inducing (GAIN) domain that contains a GPCR proteolysis site (GPS). These two features distinguish adhesion-GPCRs from other GPCR classes. Though active research on adhesion-GPCRs in diverse areas, such as immunity, neuroscience, and development and tumor biology has been intensified in the recent years, the general biological and pharmacological properties of adhesion-GPCRs are not well known, and they have not yet been used for biomedical purposes. The "6th International Adhesion-GPCR Workshop," held at the Institute of Physiology of the University of Würzburg on September 6-8, 2012, assembled a majority of the investigators currently actively pursuing research on adhesion-GPCRs, including scientists from laboratories in Europe, the United States, and Asia. The meeting featured the nascent mechanistic understanding of the molecular events driving the signal transduction of adhesion-GPCRs, novel models to evaluate their functions, and evidence for their involvement in human disease.

AB - G protein-coupled receptors (GPCRs) comprise an expanded superfamily of receptors in the human genome. Adhesion class G protein-coupled receptors (adhesion-GPCRs) form the second largest class of GPCRs. Despite the abundance, size, molecular structure, and functions in facilitating cell and matrix contacts in a variety of organ systems, adhesion-GPCRs are by far the most poorly understood GPCR class. Adhesion-GPCRs possess a unique molecular structure, with extended N-termini containing various adhesion domains. In addition, many adhesion-GPCRs are autoproteolytically cleaved into an N-terminal fragment (NTF, NT, α-subunit) and C-terminal fragment (CTF, CT, β-subunit) at a conserved GPCR autoproteolysis-inducing (GAIN) domain that contains a GPCR proteolysis site (GPS). These two features distinguish adhesion-GPCRs from other GPCR classes. Though active research on adhesion-GPCRs in diverse areas, such as immunity, neuroscience, and development and tumor biology has been intensified in the recent years, the general biological and pharmacological properties of adhesion-GPCRs are not well known, and they have not yet been used for biomedical purposes. The "6th International Adhesion-GPCR Workshop," held at the Institute of Physiology of the University of Würzburg on September 6-8, 2012, assembled a majority of the investigators currently actively pursuing research on adhesion-GPCRs, including scientists from laboratories in Europe, the United States, and Asia. The meeting featured the nascent mechanistic understanding of the molecular events driving the signal transduction of adhesion-GPCRs, novel models to evaluate their functions, and evidence for their involvement in human disease.

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KW - Humans

KW - Ligands

KW - Models, Biological

KW - Proteolysis

KW - Receptors, G-Protein-Coupled

KW - Signal Transduction

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DO - 10.1111/j.1749-6632.2012.06820.x

M3 - Journal article

C2 - 23215895

SN - 0077-8923

VL - 1276

SP - 1

EP - 25

JO - Annals of The Lyceum of Natural History of New York

JF - Annals of The Lyceum of Natural History of New York

ER -

Dissecting signaling and functions of adhesion G protein-coupled receptors

Abstract

Keywords

UN SDGs

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