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

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

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

In: Annals of the New York Academy of Sciences, Vol. 1333, 12.2014, p. 43-64.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Liebscher, I, Ackley, B, Araç, D, Ariestanti, DM, Aust, G, Bae, B, Bista, BR, Bridges, JP, Duman, JG, Engel, FB, Giera, S, Goffinet, AM, Hall, RA, Hamann, J, Hartmann, N, Lin, H-H, Liu, M, Luo, R, Mogha, A, Monk, KR, Cornelia Peeters, M, 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, pp. 43-64. https://doi.org/10.1111/nyas.12580

APA

Liebscher, I., Ackley, B., Araç, D., Ariestanti, D. M., Aust, G., Bae, B., 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, 43-64. https://doi.org/10.1111/nyas.12580

Vancouver

Liebscher I, Ackley B, Araç D, Ariestanti DM, Aust G, Bae B et al. New functions and signaling mechanisms for the class of adhesion G protein-coupled receptors. Annals of the New York Academy of Sciences. 2014 Dec;1333:43-64. https://doi.org/10.1111/nyas.12580

Author

Liebscher, Ines ; Ackley, Brian ; Araç, Demet ; Ariestanti, Donna M ; Aust, Gabriela ; Bae, Byoung-il ; Bista, Bigyan R ; Bridges, James P ; Duman, Joseph G ; Engel, Felix B ; Giera, Stefanie ; Goffinet, André M ; Hall, Randy A ; Hamann, Jörg ; Hartmann, Nicole ; Lin, Hsi-Hsien ; Liu, Mingyao ; Luo, Rong ; Mogha, Amit ; Monk, Kelly R ; Cornelia Peeters, Miriam ; Prömel, Simone ; Ressl, Susanne ; Schiöth, Helgi B ; Sigoillot, Séverine M ; Song, Helen ; Talbot, William S ; Tall, Gregory G ; White, James P ; Wolfrum, Uwe ; Xu, Lei ; Piao, Xianhua. / New functions and signaling mechanisms for the class of adhesion G protein-coupled receptors. In: Annals of the New York Academy of Sciences. 2014 ; Vol. 1333. pp. 43-64.

Bibtex

@article{d4decfbff8d14fe0ab6d336001a931d7,
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 = "Animals, Cell Adhesion, Developmental Disabilities, Humans, Mutation, Neoplasms, Receptors, G-Protein-Coupled, Signal Transduction, Synapses",
author = "Ines Liebscher and Brian Ackley and Demet Ara{\c c} and Ariestanti, {Donna M} and Gabriela Aust and Byoung-il Bae 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 Hsi-Hsien Lin and Mingyao Liu and Rong Luo and Amit Mogha and Monk, {Kelly R} and {Cornelia Peeters}, Miriam 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 = "{\textcopyright} 2014 New York Academy of Sciences.",
year = "2014",
month = dec,
doi = "10.1111/nyas.12580",
language = "English",
volume = "1333",
pages = "43--64",
journal = "Annals of The Lyceum of Natural History of New York",
issn = "0077-8923",
publisher = "Wiley-Blackwell",

}

RIS

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 - Cornelia Peeters, Miriam

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

N1 - © 2014 New York Academy of Sciences.

PY - 2014/12

Y1 - 2014/12

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 - Animals

KW - Cell Adhesion

KW - Developmental Disabilities

KW - Humans

KW - Mutation

KW - Neoplasms

KW - Receptors, G-Protein-Coupled

KW - Signal Transduction

KW - Synapses

U2 - 10.1111/nyas.12580

DO - 10.1111/nyas.12580

M3 - Journal article

C2 - 25424900

VL - 1333

SP - 43

EP - 64

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: 135484069