Phosphoproteomics using Aurora Series columns helps identify mechanisms of conformational plasticity.

G-protein-coupled receptors (GPCRs) are the largest and most diverse classes of membrane receptors in humans. These cell surface receptors act like the switchboard of the cell, communicating messages in the form of metabolites, light, peptides, lipids, sugars, and proteins. Such messages are critical for cells to survive and behave in a healthy fashion, and dysregulation of this messaging system can be causative for many diseases. Indeed, GPCRs are by far, the most therapeutically targeted class of proteins, with ~35% (>700) approved drugs targeting GPCRs both directly and indirectly.

Recent work published by Huang et. al. in Nature combined the use of Cryo-EM and phosphoproteomics to demonstrate the range of flexibility of these receptors, which is important in explaining the diverse sets of interactions they need to mediate their signals.

Read the full paper
Structure of the neurotensin receptor 1 in complex with β-arrestin 1.
Nature. 2020 Mar;579(7798):303-308. doi:
Huang W, Masureel M, Qu Q, Janetzko J, Inoue A, Kato HE, Robertson MJ, Nguyen KC, Glenn JS, Skiniotis G, Kobilka BK.

Commentary by Andrew Webb, PhD.

About the author
Andrew has over 15 years’ experience in the field of chromatography and mass spectrometry. He is the lead innovator and inventor at IonOpticks, working closely with the team to test, refine and develop cutting edge techniques to support higher quality outputs and analytics from MS instruments. Andrew is also the Lab Head of the Walter and Eliza Hall Institute of Medical Research’s Proteomics Research Laboratory.