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Abstract
The family of adhesion G protein-coupled receptors (aGPCRs) comprises 33 members in the human genome, which are subdivided into nine subclasses. Many aGPCRs undergo an autoproteolytic process via their GPCR Autoproteolysis-INducing (GAIN) domain during protein maturation to generate an N- and a C-terminal fragments, NTF and CTF, respectively. The NTF and CTF are non-covalently reassociated on the plasma membrane to form a single receptor unit. How aGPCRs are activated upon ligand binding remains one of the leading questions in the field of aGPCR research. Recent work from our labs and others shows that ligand binding can remove the NTF from the plasma membrane-bound CTF, exposing a tethered agonist which potently activates downstream signaling.
Declaration of interest
Work in our laboratories was supported in part by NIH grants R01 NS057536 (XP) and R01 NS079445 (KRM); William Randolph Hearst Fund Award (RL); Leonard and Isabelle Goldenson Research Fellowship (RL); Muscular Dystrophy Association 293295 (XP and KRM); Cerebral Palsy International Research Foundation Award (XP); Deutsche Forschungsgemeinschaft (FOR2149 to TS and IL) and the BMBF (IFB AdipositasDiseases Leipzig ADI-K767 to IL).