ArticleNature communications2026
Subtype-dependent arrestin engagement of the metabotropic glutamate receptors.
Article in Nature communications, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
2 citing papers in PubMed.
- Configurational diversity of metabotropic glutamate receptor complexes with beta-arrestins.Nature communications · 2026Article
- Structural basis of active state coupling of metabotropic glutamate receptor 8 to beta-arrestins.Nature communications · 2026Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
16 authors.
Funding
Abstract
The arrestin-mediated regulation of signaling through the metabotropic glutamate receptors (mGlus) is fundamental mechanism modulating excitatory transmission and synaptic plasticity. However, molecular details of arrestin engagement are elusive for these dimeric receptors. Here we report the structures of mGlu5 and mGlu7 bound to β-arrestin 1 (βarr1) and their endogenous agonist glutamate. The structures reveal a symmetric interaction pattern of two βarr1 molecules coupling solely to the membrane-proximal C-terminal regions of the active mGlu5, and an asymmetric binding manner with one βarr1 interacting with both transmembrane domains in the inactive mGlu7. Supported by mass spectrometry and functional data, the mGlus adopt multiple subtype-dependent arrestin binding modes that are determined by both the receptor core and C terminus. Furthermore, the activities of arrestin-mediated desensitization and endocytosis of the mGlus are likely associated with the distinct arrestin binding patterns, which may account for the differential signaling profiles of different mGlu subtypes.
Indexed as
Identifiers
What Socratic holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.