New functions and signaling mechanisms for the class of adhesion G protein-coupled receptors

Ines Liebscher; Brian Ackley; Demet Araç; Donna M. Ariestanti; Gabriela Aust; Byoung il Bae; Bigyan R. Bista; James P. Bridges; Joseph G. Duman; Felix B. Engel; Stefanie Giera; André M. Goffinet; Randy A. Hall; Jörg Hamann; Nicole Hartmann; Hsi Hsien Lin; Mingyao Liu; Rong Luo; Amit Mogha; Kelly R. Monk; Miriam C. Peeters; Simone Prömel; Susanne Ressl; Helgi B. Schiöth; Séverine M. Sigoillot; Helen Song; William S. Talbot; Gregory G. Tall; James P. White; Uwe Wolfrum; Lei Xu; Xianhua Piao

doi:10.1111/nyas.12580

New functions and signaling mechanisms for the class of adhesion G protein-coupled receptors

Ines Liebscher
, Brian Ackley
, Demet Araç
, Donna M. Ariestanti
, Gabriela Aust
, Byoung il Bae
, Bigyan R. Bista
, James P. Bridges
, Joseph G. Duman
, Felix B. Engel
, Stefanie Giera
, André M. Goffinet
, Randy A. Hall
, Jörg Hamann
, Nicole Hartmann
, Hsi Hsien Lin
, Mingyao Liu
, Rong Luo
, Amit Mogha
, Kelly R. Monk

Miriam C. Peeters, Simone Prömel, Susanne Ressl, Helgi B. Schiöth, Séverine M. Sigoillot, Helen Song, William S. Talbot, Gregory G. Tall, James P. White, Uwe Wolfrum, Lei Xu, Xianhua Piao^*

^*Corresponding author for this work

School of Life Sciences

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

25 Scopus citations

Abstract

The class of adhesion G protein-coupled receptors (aGPCRs), with 33 human homologs, is the second largest family of GPCRs. In addition to a seven-transmembrane α-helix-a structural feature of all GPCRs-the class of aGPCRs is characterized by the presence of a large N-terminal extracellular region. In addition, all aGPCRs but one (GPR123) contain a GPCR autoproteolysis-inducing (GAIN) domain that mediates autoproteolytic cleavage at the GPCR autoproteolysis site motif to generate N- and a C-terminal fragments (NTF and CTF, respectively) during protein maturation. Subsequently, the NTF and CTF are associated noncovalently as a heterodimer at the plasma membrane. While the biological function of the GAIN domain-mediated autocleavage is not fully understood, mounting evidence suggests that the NTF and CTF possess distinct biological activities in addition to their function as a receptor unit. We discuss recent advances in understanding the biological functions, signaling mechanisms, and disease associations of the aGPCRs.

Original language	English
Pages (from-to)	43-64
Number of pages	22
Journal	Annals of the New York Academy of Sciences
Volume	1333
Issue number	1
DOIs	https://doi.org/10.1111/nyas.12580
State	Published - 1 Dec 2014

Keywords

Adhesion G protein-coupled receptor
Cancer
Development
Myelination
Signal transduction
Structural biology
Synaptogenesis

UN SDGs

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

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10.1111/nyas.12580

Cite this

Liebscher, I., Ackley, B., Araç, D., Ariestanti, D. M., Aust, G., Bae, B. I., Bista, B. R., Bridges, J. P., Duman, J. G., Engel, F. B., Giera, S., Goffinet, A. M., Hall, R. A., Hamann, J., Hartmann, N., Lin, H. H., Liu, M., Luo, R., Mogha, A., ... Piao, X. (2014). New functions and signaling mechanisms for the class of adhesion G protein-coupled receptors. Annals of the New York Academy of Sciences, 1333(1), 43-64. https://doi.org/10.1111/nyas.12580

@article{98a00b0621654826a293caed0ecc7311,

title = "New functions and signaling mechanisms for the class of adhesion G protein-coupled receptors",

abstract = "The class of adhesion G protein-coupled receptors (aGPCRs), with 33 human homologs, is the second largest family of GPCRs. In addition to a seven-transmembrane α-helix-a structural feature of all GPCRs-the class of aGPCRs is characterized by the presence of a large N-terminal extracellular region. In addition, all aGPCRs but one (GPR123) contain a GPCR autoproteolysis-inducing (GAIN) domain that mediates autoproteolytic cleavage at the GPCR autoproteolysis site motif to generate N- and a C-terminal fragments (NTF and CTF, respectively) during protein maturation. Subsequently, the NTF and CTF are associated noncovalently as a heterodimer at the plasma membrane. While the biological function of the GAIN domain-mediated autocleavage is not fully understood, mounting evidence suggests that the NTF and CTF possess distinct biological activities in addition to their function as a receptor unit. We discuss recent advances in understanding the biological functions, signaling mechanisms, and disease associations of the aGPCRs.",

keywords = "Adhesion G protein-coupled receptor, Cancer, Development, Myelination, Signal transduction, Structural biology, Synaptogenesis",

author = "Ines Liebscher and Brian Ackley and Demet Ara{\c c} and Ariestanti, \{Donna M.\} and Gabriela Aust and Bae, \{Byoung il\} and Bista, \{Bigyan R.\} and Bridges, \{James P.\} and Duman, \{Joseph G.\} and Engel, \{Felix B.\} and Stefanie Giera and Goffinet, \{Andr{\'e} M.\} and Hall, \{Randy A.\} and J{\"o}rg Hamann and Nicole Hartmann and Lin, \{Hsi Hsien\} and Mingyao Liu and Rong Luo and Amit Mogha and Monk, \{Kelly R.\} and Peeters, \{Miriam C.\} and Simone Pr{\"o}mel and Susanne Ressl and Schi{\"o}th, \{Helgi B.\} and Sigoillot, \{S{\'e}verine M.\} and Helen Song and Talbot, \{William S.\} and Tall, \{Gregory G.\} and White, \{James P.\} and Uwe Wolfrum and Lei Xu and Xianhua Piao",

note = "Publisher Copyright: {\textcopyright} 2014 New York Academy of Sciences.",

year = "2014",

month = dec,

day = "1",

doi = "10.1111/nyas.12580",

language = "英语",

volume = "1333",

pages = "43--64",

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

issn = "0077-8923",

publisher = "John Wiley and Sons Inc",

number = "1",

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Liebscher, I, Ackley, B, Araç, D, Ariestanti, DM, Aust, G, Bae, BI, Bista, BR, Bridges, JP, Duman, JG, Engel, FB, Giera, S, Goffinet, AM, Hall, RA, Hamann, J, Hartmann, N, Lin, HH, Liu, M, Luo, R, Mogha, A, Monk, KR, Peeters, MC, Prömel, S, Ressl, S, Schiöth, HB, Sigoillot, SM, Song, H, Talbot, WS, Tall, GG, White, JP, Wolfrum, U, Xu, L & Piao, X 2014, 'New functions and signaling mechanisms for the class of adhesion G protein-coupled receptors', Annals of the New York Academy of Sciences, vol. 1333, no. 1, pp. 43-64. https://doi.org/10.1111/nyas.12580

TY - JOUR

T1 - New functions and signaling mechanisms for the class of adhesion G protein-coupled receptors

AU - Liebscher, Ines

AU - Ackley, Brian

AU - Araç, Demet

AU - Ariestanti, Donna M.

AU - Aust, Gabriela

AU - Bae, Byoung il

AU - Bista, Bigyan R.

AU - Bridges, James P.

AU - Duman, Joseph G.

AU - Engel, Felix B.

AU - Giera, Stefanie

AU - Goffinet, André M.

AU - Hall, Randy A.

AU - Hamann, Jörg

AU - Hartmann, Nicole

AU - Lin, Hsi Hsien

AU - Liu, Mingyao

AU - Luo, Rong

AU - Mogha, Amit

AU - Monk, Kelly R.

AU - Peeters, Miriam C.

AU - Prömel, Simone

AU - Ressl, Susanne

AU - Schiöth, Helgi B.

AU - Sigoillot, Séverine M.

AU - Song, Helen

AU - Talbot, William S.

AU - Tall, Gregory G.

AU - White, James P.

AU - Wolfrum, Uwe

AU - Xu, Lei

AU - Piao, Xianhua

PY - 2014/12/1

Y1 - 2014/12/1

N2 - The class of adhesion G protein-coupled receptors (aGPCRs), with 33 human homologs, is the second largest family of GPCRs. In addition to a seven-transmembrane α-helix-a structural feature of all GPCRs-the class of aGPCRs is characterized by the presence of a large N-terminal extracellular region. In addition, all aGPCRs but one (GPR123) contain a GPCR autoproteolysis-inducing (GAIN) domain that mediates autoproteolytic cleavage at the GPCR autoproteolysis site motif to generate N- and a C-terminal fragments (NTF and CTF, respectively) during protein maturation. Subsequently, the NTF and CTF are associated noncovalently as a heterodimer at the plasma membrane. While the biological function of the GAIN domain-mediated autocleavage is not fully understood, mounting evidence suggests that the NTF and CTF possess distinct biological activities in addition to their function as a receptor unit. We discuss recent advances in understanding the biological functions, signaling mechanisms, and disease associations of the aGPCRs.

AB - The class of adhesion G protein-coupled receptors (aGPCRs), with 33 human homologs, is the second largest family of GPCRs. In addition to a seven-transmembrane α-helix-a structural feature of all GPCRs-the class of aGPCRs is characterized by the presence of a large N-terminal extracellular region. In addition, all aGPCRs but one (GPR123) contain a GPCR autoproteolysis-inducing (GAIN) domain that mediates autoproteolytic cleavage at the GPCR autoproteolysis site motif to generate N- and a C-terminal fragments (NTF and CTF, respectively) during protein maturation. Subsequently, the NTF and CTF are associated noncovalently as a heterodimer at the plasma membrane. While the biological function of the GAIN domain-mediated autocleavage is not fully understood, mounting evidence suggests that the NTF and CTF possess distinct biological activities in addition to their function as a receptor unit. We discuss recent advances in understanding the biological functions, signaling mechanisms, and disease associations of the aGPCRs.

KW - Adhesion G protein-coupled receptor

KW - Cancer

KW - Development

KW - Myelination

KW - Signal transduction

KW - Structural biology

KW - Synaptogenesis

UR - https://www.scopus.com/pages/publications/84919657032

U2 - 10.1111/nyas.12580

DO - 10.1111/nyas.12580

M3 - 文章

C2 - 25424900

AN - SCOPUS:84919657032

SN - 0077-8923

VL - 1333

SP - 43

EP - 64

JO - Annals of the New York Academy of Sciences

JF - Annals of the New York Academy of Sciences

IS - 1

ER -

New functions and signaling mechanisms for the class of adhesion G protein-coupled receptors

Abstract

Keywords

UN SDGs

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