The expanding functional roles and signaling mechanisms of adhesion g protein–coupled receptors

Rory K. Morgan; Garret R. Anderson; Demet Araç; Gabriela Aust; Nariman Balenga; Antony Boucard; James P. Bridges; Felix B. Engel; Caroline J. Formstone; Maike D. Glitsch; Ryan S. Gray; Randy A. Hall; Cheng Chih Hsiao; Hee Yong Kim; Alexander B. Knierim; Deva Krupakar Kusuluri; Katherine Leon; Ines Liebscher; Xianhua Piao; Simone Prömel; Nicole Scholz; Swati Srivastava; Doreen Thor; Kimberley F. Tolias; Yuri A. Ushkaryov; Mario Vallon; Erwin G. Van Meir; Benoit Vanhollebeke; Uwe Wolfrum; Kevin M. Wright; Kelly R. Monk; Amit Mogha

doi:10.1111/nyas.14094

The expanding functional roles and signaling mechanisms of adhesion g protein–coupled receptors

Rory K. Morgan, Garret R. Anderson, Demet Araç, Gabriela Aust, Nariman Balenga, Antony Boucard, James P. Bridges, Felix B. Engel, Caroline J. Formstone, Maike D. Glitsch, Ryan S. Gray, Randy A. Hall, Cheng Chih Hsiao, Hee Yong Kim, Alexander B. Knierim, Deva Krupakar Kusuluri, Katherine Leon, Ines Liebscher, Xianhua Piao, Simone PrömelNicole Scholz, Swati Srivastava, Doreen Thor, Kimberley F. Tolias, Yuri A. Ushkaryov, Mario Vallon, Erwin G. Van Meir, Benoit Vanhollebeke, Uwe Wolfrum, Kevin M. Wright, Kelly R. Monk, Amit Mogha

Vollum Institute

Research output: Chapter in Book/Report/Conference proceeding › Chapter

12 Scopus citations

Abstract

The adhesion class of G protein–coupled receptors (GPCRs) is the second largest family of GPCRs (33 members in humans). Adhesion GPCRs (aGPCRs) are defined by a large extracellular N-terminal region that is linked to a C-terminal seven transmembrane (7TM) domain via a GPCR-autoproteolysis inducing (GAIN) domain containing a GPCR proteolytic site (GPS). Most aGPCRs undergo autoproteolysis at the GPS motif, but the cleaved fragments stay closely associated, with the N-terminal fragment (NTF) bound to the 7TM of the C-terminal fragment (CTF). The NTFs of most aGPCRs contain domains known to be involved in cell–cell adhesion, while the CTFs are involved in classical G protein signaling, as well as other intracellular signaling. In this workshop report, we review the most recent findings on the biology, signaling mechanisms, and physiological functions of aGPCRs.

Original language	English (US)
Title of host publication	Annals of the New York Academy of Sciences
Publisher	Blackwell Publishing Inc.
Pages	5-25
Number of pages	21
Edition	1
DOIs	https://doi.org/10.1111/nyas.14094
State	Published - 2019

Publication series

Name	Annals of the New York Academy of Sciences
Number	1
Volume	1456
ISSN (Print)	0077-8923
ISSN (Electronic)	1749-6632

Keywords

Adhesion G protein
Cancer
Coupled receptor
Development
Immunology
Mechanosensation
Neurobiology
Signal transduction
Structural biology

ASJC Scopus subject areas

General Neuroscience
General Biochemistry, Genetics and Molecular Biology
History and Philosophy of Science

Access to Document

10.1111/nyas.14094

Cite this

Morgan, R. K., Anderson, G. R., Araç, D., Aust, G., Balenga, N., Boucard, A., Bridges, J. P., Engel, F. B., Formstone, C. J., Glitsch, M. D., Gray, R. S., Hall, R. A., Hsiao, C. C., Kim, H. Y., Knierim, A. B., Kusuluri, D. K., Leon, K., Liebscher, I., Piao, X., ... Mogha, A. (2019). The expanding functional roles and signaling mechanisms of adhesion g protein–coupled receptors. In Annals of the New York Academy of Sciences (1 ed., pp. 5-25). (Annals of the New York Academy of Sciences; Vol. 1456, No. 1). Blackwell Publishing Inc.. https://doi.org/10.1111/nyas.14094

The expanding functional roles and signaling mechanisms of adhesion g protein–coupled receptors. / Morgan, Rory K.; Anderson, Garret R.; Araç, Demet et al.
Annals of the New York Academy of Sciences. 1. ed. Blackwell Publishing Inc., 2019. p. 5-25 (Annals of the New York Academy of Sciences; Vol. 1456, No. 1).

Research output: Chapter in Book/Report/Conference proceeding › Chapter

Morgan, RK, Anderson, GR, Araç, D, Aust, G, Balenga, N, Boucard, A, Bridges, JP, Engel, FB, Formstone, CJ, Glitsch, MD, Gray, RS, Hall, RA, Hsiao, CC, Kim, HY, Knierim, AB, Kusuluri, DK, Leon, K, Liebscher, I, Piao, X, Prömel, S, Scholz, N, Srivastava, S, Thor, D, Tolias, KF, Ushkaryov, YA, Vallon, M, Van Meir, EG, Vanhollebeke, B, Wolfrum, U, Wright, KM , Monk, KR & Mogha, A 2019, The expanding functional roles and signaling mechanisms of adhesion g protein–coupled receptors. in Annals of the New York Academy of Sciences. 1 edn, Annals of the New York Academy of Sciences, no. 1, vol. 1456, Blackwell Publishing Inc., pp. 5-25. https://doi.org/10.1111/nyas.14094

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title = "The expanding functional roles and signaling mechanisms of adhesion g protein–coupled receptors",

abstract = "The adhesion class of G protein–coupled receptors (GPCRs) is the second largest family of GPCRs (33 members in humans). Adhesion GPCRs (aGPCRs) are defined by a large extracellular N-terminal region that is linked to a C-terminal seven transmembrane (7TM) domain via a GPCR-autoproteolysis inducing (GAIN) domain containing a GPCR proteolytic site (GPS). Most aGPCRs undergo autoproteolysis at the GPS motif, but the cleaved fragments stay closely associated, with the N-terminal fragment (NTF) bound to the 7TM of the C-terminal fragment (CTF). The NTFs of most aGPCRs contain domains known to be involved in cell–cell adhesion, while the CTFs are involved in classical G protein signaling, as well as other intracellular signaling. In this workshop report, we review the most recent findings on the biology, signaling mechanisms, and physiological functions of aGPCRs.",

keywords = "Adhesion G protein, Cancer, Coupled receptor, Development, Immunology, Mechanosensation, Neurobiology, Signal transduction, Structural biology",

author = "Morgan, {Rory K.} and Anderson, {Garret R.} and Demet Ara{\c c} and Gabriela Aust and Nariman Balenga and Antony Boucard and Bridges, {James P.} and Engel, {Felix B.} and Formstone, {Caroline J.} and Glitsch, {Maike D.} and Gray, {Ryan S.} and Hall, {Randy A.} and Hsiao, {Cheng Chih} and Kim, {Hee Yong} and Knierim, {Alexander B.} and Kusuluri, {Deva Krupakar} and Katherine Leon and Ines Liebscher and Xianhua Piao and Simone Pr{\"o}mel and Nicole Scholz and Swati Srivastava and Doreen Thor and Tolias, {Kimberley F.} and Ushkaryov, {Yuri A.} and Mario Vallon and {Van Meir}, {Erwin G.} and Benoit Vanhollebeke and Uwe Wolfrum and Wright, {Kevin M.} and Monk, {Kelly R.} and Amit Mogha",

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AU - Anderson, Garret R.

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AU - Balenga, Nariman

AU - Boucard, Antony

AU - Bridges, James P.

AU - Engel, Felix B.

AU - Formstone, Caroline J.

AU - Glitsch, Maike D.

AU - Gray, Ryan S.

AU - Hall, Randy A.

AU - Hsiao, Cheng Chih

AU - Kim, Hee Yong

AU - Knierim, Alexander B.

AU - Kusuluri, Deva Krupakar

AU - Leon, Katherine

AU - Liebscher, Ines

AU - Piao, Xianhua

AU - Prömel, Simone

AU - Scholz, Nicole

AU - Srivastava, Swati

AU - Thor, Doreen

AU - Tolias, Kimberley F.

AU - Ushkaryov, Yuri A.

AU - Vallon, Mario

AU - Van Meir, Erwin G.

AU - Vanhollebeke, Benoit

AU - Wolfrum, Uwe

AU - Wright, Kevin M.

AU - Monk, Kelly R.

AU - Mogha, Amit

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N2 - The adhesion class of G protein–coupled receptors (GPCRs) is the second largest family of GPCRs (33 members in humans). Adhesion GPCRs (aGPCRs) are defined by a large extracellular N-terminal region that is linked to a C-terminal seven transmembrane (7TM) domain via a GPCR-autoproteolysis inducing (GAIN) domain containing a GPCR proteolytic site (GPS). Most aGPCRs undergo autoproteolysis at the GPS motif, but the cleaved fragments stay closely associated, with the N-terminal fragment (NTF) bound to the 7TM of the C-terminal fragment (CTF). The NTFs of most aGPCRs contain domains known to be involved in cell–cell adhesion, while the CTFs are involved in classical G protein signaling, as well as other intracellular signaling. In this workshop report, we review the most recent findings on the biology, signaling mechanisms, and physiological functions of aGPCRs.

AB - The adhesion class of G protein–coupled receptors (GPCRs) is the second largest family of GPCRs (33 members in humans). Adhesion GPCRs (aGPCRs) are defined by a large extracellular N-terminal region that is linked to a C-terminal seven transmembrane (7TM) domain via a GPCR-autoproteolysis inducing (GAIN) domain containing a GPCR proteolytic site (GPS). Most aGPCRs undergo autoproteolysis at the GPS motif, but the cleaved fragments stay closely associated, with the N-terminal fragment (NTF) bound to the 7TM of the C-terminal fragment (CTF). The NTFs of most aGPCRs contain domains known to be involved in cell–cell adhesion, while the CTFs are involved in classical G protein signaling, as well as other intracellular signaling. In this workshop report, we review the most recent findings on the biology, signaling mechanisms, and physiological functions of aGPCRs.

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KW - Cancer

KW - Coupled receptor

KW - Development

KW - Immunology

KW - Mechanosensation

KW - Neurobiology

KW - Signal transduction

KW - Structural biology

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BT - Annals of the New York Academy of Sciences

PB - Blackwell Publishing Inc.

ER -

The expanding functional roles and signaling mechanisms of adhesion g protein–coupled receptors

Abstract

Publication series

Keywords

ASJC Scopus subject areas

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