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Fast-diffusing receptor collisions with slow-diffusing peptide ligand assemble the ternary parathyroid hormone-GPCR-arrestin complex. | LitMetric

AI Article Synopsis

  • - The study investigates how a peptide hormone (PTH) interacts with its receptor (PTHR) and β-arrestin (βarr) to form a ternary complex, which is key for G protein-coupled receptor (GPCR) signaling.
  • - Using fluorescent markers and advanced imaging techniques, the research shows that PTHR moves freely in the cell membrane while unbound PTH has limited mobility, indicating a distinct dynamic behavior.
  • - The formation of the PTH-PTHR-βarr complex happens in three steps: ligand-receptor collisions, βarr recruitment triggered by a specific lipid (PIP), and final assembly within clathrin clusters, highlighting the importance of PIP in GPCR

Article Abstract

The assembly of a peptide ligand, its receptor, and β-arrestin (βarr) into a ternary complex within the cell membrane is a crucial aspect of G protein-coupled receptor (GPCR) signaling. We explore this assembly by attaching fluorescent moieties to the parathyroid hormone (PTH) type 1 receptor (PTHR), using PTH as a prototypical peptide hormone, along with βarr and clathrin, and recording dual-color single-molecule imaging at the plasma membrane of live cells. Here we show that PTHR exhibits a near-Brownian diffusion, whereas unbound hormone displays limited mobility and slow lateral diffusion at the cell surface. The formation of the PTH-PTHR-βarr complex occurs in three sequential steps: (1) receptor and ligand collisions, (2) phosphoinositide (PIP)-dependent recruitment and conformational change of βarr molecules at the plasma membrane, and (3) collision of most βarr molecules with the ligand-bound receptor within clathrin clusters. Our results elucidate the non-random pathway by which PTH-PTHR-βarr complex is formed and unveil the critical role of PIP in regulating GPCR signaling.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC11615292PMC
http://dx.doi.org/10.1038/s41467-024-54772-3DOI Listing

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