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Structure of the neurotensin receptor 1 in complex with β-arrestin 1
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Structure of the neurotensin receptor 1 in complex with β-arrestin 1
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Journal Article
Structure of the neurotensin receptor 1 in complex with β-arrestin 1
2020
Overview
Arrestin proteins bind to active, phosphorylated G-protein-coupled receptors (GPCRs), thereby preventing G-protein coupling, triggering receptor internalization and affecting various downstream signalling pathways
1
,
2
. Although there is a wealth of structural information detailing the interactions between GPCRs and G proteins, less is known about how arrestins engage GPCRs. Here we report a cryo-electron microscopy structure of full-length human neurotensin receptor 1 (NTSR1) in complex with truncated human β-arrestin 1 (βarr1(ΔCT)). We find that phosphorylation of NTSR1 is critical for the formation of a stable complex with βarr1(ΔCT), and identify phosphorylated sites in both the third intracellular loop and the C terminus that may promote this interaction. In addition, we observe a phosphatidylinositol-4,5-bisphosphate molecule forming a bridge between the membrane side of NTSR1 transmembrane segments 1 and 4 and the C-lobe of arrestin. Compared with a structure of a rhodopsin–arrestin-1 complex, in our structure arrestin is rotated by approximately 85° relative to the receptor. These findings highlight both conserved aspects and plasticity among arrestin–receptor interactions.
A cryo-electron microscopy structure of the neurotensin receptor 1 in complex with β-arrestin 1 is reported.
Publisher
Nature Publishing Group UK,Nature Publishing Group
Subject
/ 82
/ 82/16
/ 82/58
/ 82/80
/ 82/83
/ 96
/ 96/95
/ Arrestin
/ beta-Arrestin 1 - metabolism
/ Humanities and Social Sciences
/ Humans
/ Kinases
/ Phosphatidylinositol 4,5-diphosphate
/ Protein Structure, Quaternary
/ Proteins
/ Receptors, Neurotensin - chemistry
/ Receptors, Neurotensin - metabolism
/ Science
