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- W4384663453 abstract "Abstract Adhesion G protein‐coupled receptors (aGPCRs) possess a unique topology, including the presence of a GPCR proteolysis site (GPS), which, upon autoproteolysis, generates two functionally distinct fragments that remain non‐covalently associated at the plasma membrane. A proposed activation mechanism for aGPCRs involves the exposure of a tethered agonist, which depends on cleavage at the GPS. However, this hypothesis has been challenged by the observation that non‐cleavable aGPCRs exhibit constitutive activity, thus making the function of GPS cleavage widely enigmatic. In this study, we sought to elucidate the function of GPS‐mediated cleavage through the study of G protein coupling with Latrophilin‐3/ADGRL3, a prototypical aGPCR involved in synapse formation and function. Using BRET‐based G protein biosensors, we reveal that an autoproteolysis‐deficient mutant of ADGRL3 retains constitutive activity. Surprisingly, we uncover that cleavage deficiency leads to a signalling bias directed at potentiating the activity of select G proteins such as Gi2 and G12/13. These data unveil the underpinnings of biased signalling for aGPCRs defined by GPS autoproteolysis." @default.
- W4384663453 created "2023-07-20" @default.
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- W4384663453 date "2023-08-01" @default.
- W4384663453 modified "2023-10-17" @default.
- W4384663453 title "Biased signalling is structurally encoded as an autoproteolysis event in adhesion G protein‐coupled receptor Latrophilin‐3/ADGRL3" @default.
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- W4384663453 doi "https://doi.org/10.1111/bcpt.13927" @default.
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