Dissecting signaling and functions of adhesion G protein-coupled receptors

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

SN - 0077-8923

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

ER -