Tethered agonists: a new mechanism underlying adhesion G protein-coupled receptor activation. (4th May 2015)

• Record Type: Journal Article
• Authors: Schöneberg, Torsten; Liebscher, Ines; Luo, Rong; Monk, Kelly R.; Piao, Xianhua
• Is Part Of: Journal of receptor and signal transduction research. Volume 35:Number 3(2015)
• Page Start: 220
• Page End: 223
• Publication Date: 2015-05-04
• Subjects: adhesion GPCR -- tethered agonist -- G protein-coupled signaling; Cell receptors -- Periodicals; Cellular signal transduction -- Periodicals; 571.6
• DOI: 10.3109/10799893.2015.1072978
• Languages: English
• ISSNs: 1079-9893

Abstract

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 G PCR A utoproteolysis- IN ducing (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.