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The expanding functional roles and signaling mechanisms of adhesion G protein-coupled receptors.

par Morgan, Rory K;Anderson, Garret R;Araç, Demet;Aust, Gabriela;Balenga, Nariman;Boucard, Antony;Bridges, James P;Engel, Felix B;Formstone, Caroline CJ;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, Benoît ;Wolfrum, Uwe;Wright, Kevin M;Monk, Kelly R;Mogha, Amit
Référence Annals of the New York Academy of Sciences
Publication Publié, 2019-06-01

Article révisé par les pairs

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Résumé :

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.