Dissecting signaling and functions of adhesion G protein-coupled receptors

Research output: Contribution to journalJournal articleResearchpeer-review

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

In: Annals of the New York Academy of Sciences, Vol. 1276, 12.2012, p. 1-25.

Research output: Contribution to journalJournal articleResearchpeer-review

Harvard

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

APA

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

Vancouver

Araç D, Aust G, Calebiro D, Engel FB, Formstone C, Goffinet A et al. Dissecting signaling and functions of adhesion G protein-coupled receptors. Annals of the New York Academy of Sciences. 2012 Dec;1276:1-25. https://doi.org/10.1111/j.1749-6632.2012.06820.x

Author

Araç, Demet ; Aust, Gabriela ; Calebiro, Davide ; Engel, Felix B ; Formstone, Caroline ; Goffinet, André ; Hamann, Jörg ; Kittel, Robert J ; Liebscher, Ines ; Lin, Hsi-Hsien ; Monk, Kelly R ; Petrenko, Alexander ; Piao, Xianhua ; Prömel, Simone ; Schiöth, Helgi B ; Schwartz, Thue W. ; Stacey, Martin ; Ushkaryov, Yuri A ; Wobus, Manja ; Wolfrum, Uwe ; Xu, Lei ; Langenhan, Tobias. / Dissecting signaling and functions of adhesion G protein-coupled receptors. In: Annals of the New York Academy of Sciences. 2012 ; Vol. 1276. pp. 1-25.

Bibtex

@article{a529c8f91aa143bebdd373a0c563488f,
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, 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 W{\"u}rzburg 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 = "Cell Adhesion, Humans, Ligands, Models, Biological, Proteolysis, Receptors, G-Protein-Coupled, Signal Transduction",
author = "Demet Ara{\c c} and Gabriela Aust and Davide Calebiro and Engel, {Felix B} and Caroline Formstone and Andr{\'e} Goffinet and J{\"o}rg Hamann and Kittel, {Robert J} and Ines Liebscher and Hsi-Hsien Lin and Monk, {Kelly R} and Alexander Petrenko and Xianhua Piao and Simone Pr{\"o}mel and Schi{\"o}th, {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",
note = "{\textcopyright} 2012 New York Academy of Sciences.",
year = "2012",
month = dec,
doi = "10.1111/j.1749-6632.2012.06820.x",
language = "English",
volume = "1276",
pages = "1--25",
journal = "Annals of The Lyceum of Natural History of New York",
issn = "0077-8923",
publisher = "Wiley-Blackwell",

}

RIS

TY - JOUR

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

N1 - © 2012 New York Academy of Sciences.

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.

KW - Cell Adhesion

KW - Humans

KW - Ligands

KW - Models, Biological

KW - Proteolysis

KW - Receptors, G-Protein-Coupled

KW - Signal Transduction

U2 - 10.1111/j.1749-6632.2012.06820.x

DO - 10.1111/j.1749-6632.2012.06820.x

M3 - Journal article

C2 - 23215895

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

SN - 0077-8923

ER -

ID: 137294388