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- W3158708184 endingPage "109050" @default.
- W3158708184 startingPage "109050" @default.
- W3158708184 abstract "G protein-coupled receptors (GPCRs) interact with intracellular transducers to control both signal initiation and desensitization, but the distinct mechanisms that control the regulation of different GPCR subtypes are unclear. Here we use fluorescence imaging and electrophysiology to examine the metabotropic glutamate receptor (mGluR) family. We find distinct properties across subtypes in both rapid desensitization and internalization, with striking differences between the group II mGluRs. mGluR3, but not mGluR2, undergoes glutamate-dependent rapid desensitization, internalization, trafficking, and recycling. We map differences between mGluRs to variable Ser/Thr-rich sequences in the C-terminal domain (CTD) that control interaction with both GPCR kinases and β-arrestins. Finally, we identify a cancer-associated mutation, G848E, within the mGluR3 CTD that enhances β-arrestin coupling and internalization, enabling an analysis of mGluR3 β-arrestin-coupling properties and revealing biased variants. Together, this work provides a framework for understanding the distinct regulation and functional roles of mGluR subtypes." @default.
- W3158708184 created "2021-05-10" @default.
- W3158708184 creator A5015188394 @default.
- W3158708184 creator A5029100534 @default.
- W3158708184 creator A5031211334 @default.
- W3158708184 creator A5052828192 @default.
- W3158708184 date "2021-04-01" @default.
- W3158708184 modified "2023-10-15" @default.
- W3158708184 title "Mechanisms of differential desensitization of metabotropic glutamate receptors" @default.
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