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^*

^*此作品的通讯作者

生命科学学院

Institute of Biochemistry
Leipzig University
Department of Molecular Biosciences
University of Kansas
The University of Chicago
Department of Biological Sciences
Institute of Science Tokyo
Department of Surgery
Division of Genetics and Genomics
Boston Children's Hospital
Massachusetts Institute of Technology
Perinatal Institute
Cincinnati Children's Hospital Medical Center
Department of Neuroscience
Baylor College of Medicine
Department of Pathology
Friedrich-Alexander University Erlangen-Nürnberg
Division of Newborn Medicine
Developmental Neurobiology
Université catholique de Louvain
Department of Pharmacology
Emory University
Department of Experimental Immunology
University of Amsterdam
Department of Neurophysiology
University of Würzburg
Department of Microbiology and Immunology
Chang Gung University
Department of Developmental Biology
Washington University St. Louis
Section for Metabolic Receptology and Enteroendocrinology
University of Copenhagen
Department of Molecular and Cellular Physiology
Stanford University
Department of Neuroscience
Uppsala University
Collège de France
Schepens Eye Research Institute
Department of Developmental Biology
Department of Pharmacology and Physiology
University of Rochester
Department of Cell Biology
Harvard University
Cell and Matrix Biology
Johannes Gutenberg University Mainz
Department of Dermatology

科研成果: 期刊稿件 › 文章 › 同行评审

28 引用（Scopus）

摘要

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.

源语言	英语
页（从-至）	43-64
页数	22
期刊	Annals of the New York Academy of Sciences
卷	1333
期	1
DOI	https://doi.org/10.1111/nyas.12580
出版状态	已出版 - 1 12月 2014

联合国可持续发展目标

此成果有助于实现下列可持续发展目标：

可持续发展目标 3 良好健康与福祉

访问文件

10.1111/nyas.12580

其它文件与链接

链接到 Scopus 的出版物

引用此

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",

}

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, 卷 1333, 号码 1, 页码 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

摘要

联合国可持续发展目标

访问文件

其它文件与链接

学术指纹

引用此