Journal: Cell / Year: 2023 Title: Negative allosteric modulation of the glucagon receptor by RAMP2. Authors: Kaavya Krishna Kumar / Evan S O'Brien / Chris H Habrian / Naomi R Latorraca / Haoqing Wang / Inga Tuneew / Elizabeth Montabana / Susan Marqusee / Daniel Hilger / Ehud Y Isacoff / Jesper ...Authors: Kaavya Krishna Kumar / Evan S O'Brien / Chris H Habrian / Naomi R Latorraca / Haoqing Wang / Inga Tuneew / Elizabeth Montabana / Susan Marqusee / Daniel Hilger / Ehud Y Isacoff / Jesper Mosolff Mathiesen / Brian K Kobilka / Abstract: Receptor activity-modifying proteins (RAMPs) modulate the activity of many Family B GPCRs. We show that RAMP2 directly interacts with the glucagon receptor (GCGR), a Family B GPCR responsible for ...Receptor activity-modifying proteins (RAMPs) modulate the activity of many Family B GPCRs. We show that RAMP2 directly interacts with the glucagon receptor (GCGR), a Family B GPCR responsible for blood sugar homeostasis, and broadly inhibits receptor-induced downstream signaling. HDX-MS experiments demonstrate that RAMP2 enhances local flexibility in select locations in and near the receptor extracellular domain (ECD) and in the 6 transmembrane helix, whereas smFRET experiments show that this ECD disorder results in the inhibition of active and intermediate states of the intracellular surface. We determined the cryo-EM structure of the GCGR-G complex at 2.9 Å resolution in the presence of RAMP2. RAMP2 apparently does not interact with GCGR in an ordered manner; however, the receptor ECD is indeed largely disordered along with rearrangements of several intracellular hallmarks of activation. Our studies suggest that RAMP2 acts as a negative allosteric modulator of GCGR by enhancing conformational sampling of the ECD.
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