Dissecting signaling and functions of adhesion G protein-coupled receptors

Demet Arac; Gabriela Aust; Davide Calebiro; Felix B. Engel; Caroline Formstone; Andre Goffinet; Joerg Hamann; Robert J. Kittel; Ines Liebscher; Hsi-Hsien Lin; Kelly R. Monk; Alexander Petrenko; Xianhua Piao; Simone Proemel; Helgi B. Schioth; 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 Arac, Gabriela Aust, Davide Calebiro, Felix B. Engel, Caroline Formstone, Andre Goffinet, Joerg Hamann, Robert J. Kittel, Ines Liebscher, Hsi-Hsien Lin, Kelly R. Monk, Alexander Petrenko, Xianhua Piao, Simone Proemel, Helgi B. Schioth, Thue W. Schwartz, Martin Stacey, Yuri A. Ushkaryov, Manja Wobus, Uwe WolfrumLei Xu, Tobias Langenhan^*

^*Corresponding author for this work

Developmental Neurobiology

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

36 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, alpha-subunit) and C-terminal fragment (CTF, CT, beta-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 Wurzburg 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
Article number	N/A
Pages (from-to)	1-25
Number of pages	25
Journal	Annals of the New York Academy of Sciences
Volume	1276
Issue number	N/A
DOIs	https://doi.org/10.1111/j.1749-6632.2012.06820.x
Publication status	Published - Dec 2012

Keywords

G protein-coupled receptors
GPS motif
autoproteolysis
molecular and genetic analysis
CALCIUM-INDEPENDENT RECEPTOR
ALPHA-LATROTOXIN-BINDING
PLANAR CELL POLARITY
PROTEOLYTIC CLEAVAGE
ENDOTHELIAL-CELLS
PROGENITOR-CELL
TISSUE POLARITY
GPCR EMR2
CD97
GPR56

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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Arac, 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., Proemel, S., Schioth, 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(N/A), 1-25. Article N/A. https://doi.org/10.1111/j.1749-6632.2012.06820.x

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title = "Dissecting signaling and functions of adhesion G protein-coupled receptors",

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, alpha-subunit) and C-terminal fragment (CTF, CT, beta-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 Wurzburg 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.",

keywords = "G protein-coupled receptors, GPS motif, autoproteolysis, molecular and genetic analysis, CALCIUM-INDEPENDENT RECEPTOR, ALPHA-LATROTOXIN-BINDING, PLANAR CELL POLARITY, PROTEOLYTIC CLEAVAGE, ENDOTHELIAL-CELLS, PROGENITOR-CELL, TISSUE POLARITY, GPCR EMR2, CD97, GPR56",

author = "Demet Arac and Gabriela Aust and Davide Calebiro and Engel, {Felix B.} and Caroline Formstone and Andre Goffinet and Joerg Hamann and Kittel, {Robert J.} and Ines Liebscher and Hsi-Hsien Lin and Monk, {Kelly R.} and Alexander Petrenko and Xianhua Piao and Simone Proemel and Schioth, {Helgi B.} and Schwartz, {Thue W.} and Martin Stacey and Ushkaryov, {Yuri A.} and Manja Wobus and Uwe Wolfrum and Lei Xu and Tobias Langenhan",

year = "2012",

month = dec,

doi = "10.1111/j.1749-6632.2012.06820.x",

language = "English",

volume = "1276",

pages = "1--25",

journal = "Annals of the New York Academy of Sciences",

issn = "0077-8923",

publisher = "Wiley-Blackwell",

number = "N/A",

}

Arac, 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, Proemel, S, Schioth, 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, no. N/A, N/A, pp. 1-25. https://doi.org/10.1111/j.1749-6632.2012.06820.x

TY - JOUR

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

AU - Arac, Demet

AU - Aust, Gabriela

AU - Calebiro, Davide

AU - Engel, Felix B.

AU - Formstone, Caroline

AU - Goffinet, Andre

AU - Hamann, Joerg

AU - Kittel, Robert J.

AU - Liebscher, Ines

AU - Lin, Hsi-Hsien

AU - Monk, Kelly R.

AU - Petrenko, Alexander

AU - Piao, Xianhua

AU - Proemel, Simone

AU - Schioth, 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, alpha-subunit) and C-terminal fragment (CTF, CT, beta-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 Wurzburg 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, alpha-subunit) and C-terminal fragment (CTF, CT, beta-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 Wurzburg 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.

KW - G protein-coupled receptors

KW - GPS motif

KW - autoproteolysis

KW - molecular and genetic analysis

KW - CALCIUM-INDEPENDENT RECEPTOR

KW - ALPHA-LATROTOXIN-BINDING

KW - PLANAR CELL POLARITY

KW - PROTEOLYTIC CLEAVAGE

KW - ENDOTHELIAL-CELLS

KW - PROGENITOR-CELL

KW - TISSUE POLARITY

KW - GPCR EMR2

KW - CD97

KW - GPR56

U2 - 10.1111/j.1749-6632.2012.06820.x

DO - 10.1111/j.1749-6632.2012.06820.x

M3 - Article

SN - 0077-8923

VL - 1276

SP - 1

EP - 25

JO - Annals of the New York Academy of Sciences

JF - Annals of the New York Academy of Sciences

IS - N/A

M1 - N/A

ER -

Dissecting signaling and functions of adhesion G protein-coupled receptors

Abstract

Keywords

UN SDGs

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