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