Photoinduced receptor confinement drives ligand-independent GPCR signaling

Cell-cell communication relies on the assembly of receptor-ligand complexes at the plasma membrane. The spatiotemporal receptor organization has a pivotal role in evoking cellular responses. We studied the clustering of heterotrimeric guanine nucleotide-binding protein (G protein)-coupled receptors...

Full description

Saved in:
Bibliographic Details
Published in:Science (American Association for the Advancement of Science) 2021-03, Vol.371 (6536)
Main Authors: Sánchez, M Florencia, Els-Heindl, Sylvia, Beck-Sickinger, Annette G, Wieneke, Ralph, Tampé, Robert
Format: Article
Language:English
Subjects:
Affinity
Assembly
Calcium
Calcium - metabolism
Calcium Signaling
Cell adhesion & migration
Cell Line
Cell Membrane - metabolism
Cell Movement
Cells (biology)
Chelating agents
Clustering
Confinement
Coordination compounds
Copolymers
Cytosol - metabolism
Diffusion
Epilepsy
G protein-coupled receptors
Graft copolymers
Histidine
Human performance
Humans
Laser applications
Lasers
Ligands
Light
Lipids - analysis
Luminous intensity
Lysine
Membranes
Models, Biological
Motility
Neuropeptide Y - pharmacology
Neuropeptides
Nitrilotriacetic acid
Nucleotides
Photoactivation
Physiology
Proteins
Receptor Aggregation
Receptors, Neuropeptide Y - agonists
Receptors, Neuropeptide Y - antagonists & inhibitors
Receptors, Neuropeptide Y - metabolism
Residential density
Signal Transduction
Spatial distribution
Stability
Topology
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Cell-cell communication relies on the assembly of receptor-ligand complexes at the plasma membrane. The spatiotemporal receptor organization has a pivotal role in evoking cellular responses. We studied the clustering of heterotrimeric guanine nucleotide-binding protein (G protein)-coupled receptors (GPCRs) and established a photoinstructive matrix with ultrasmall lock-and-key interaction pairs to control lateral membrane organization of hormone neuropeptide Y receptors in living cells by light. Within seconds, receptor clustering was modulated in size, location, and density. After in situ confinement, changes in cellular morphology, motility, and calcium signaling revealed ligand-independent receptor activation. This approach may enhance the exploration of mechanisms in cell signaling and mechanotransduction.
ISSN:0036-8075
1095-9203
DOI:10.1126/science.abb7657