ArticleCellular and molecular life sciences : CMLS2015
Kir3 channels undergo arrestin-dependant internalization following delta opioid receptor activation.
Article in Cellular and molecular life sciences : CMLS, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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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.
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Who cites it
10 citing papers in PubMed.
- Opioid receptors signaling network.Journal of cell communication and signaling · 2022Article
- Review
- Agonist-induced phosphorylation bar code and differential post-activation signaling of the delta opioid receptor revealed by phosphosite-specific antibodies.Scientific reports · 2020Article
- Vitamin D and Its Potential Interplay With Pain Signaling Pathways.Frontiers in immunology · 2020Review
- The Delta-Opioid Receptor; a Target for the Treatment of Pain.Frontiers in molecular neuroscience · 2020Review
- Encoding the β-Arrestin Trafficking Fate of Ghrelin Receptor GHSR1a: C-Tail-Independent Molecular Determinants in GPCRs.ACS pharmacology & translational science · 2019Article
- Tolerance to high-internalizing δ opioid receptor agonist is critically mediated by arrestin 2.British journal of pharmacology · 2018Article
- Delta opioid receptors recycle to the membrane after sorting to the degradation path.Cellular and molecular life sciences : CMLS · 2018Article
- The delta opioid receptor tool box.Neuroscience · 2016Review
- Molecular Pharmacology of δ-Opioid Receptors.Pharmacological reviews · 2016Review
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Kir3 channels control excitability in the nervous system and the heart. Their surface expression is strictly regulated, but mechanisms responsible for channel removal from the membrane remain incompletely understood. Using transfected cells, we show that Kir3.1/3.2 channels and delta opioid receptors (DORs) associate in a complex which persists during receptor activation, behaving as a scaffold that allows beta-arrestin (βarr) to interact with both signaling partners. This organization favored co-internalization of DORs and Kir3 channels in a βarr-dependent manner via a clathrin/dynamin-mediated endocytic path. Taken together, these findings identify a new way of modulating Kir3 channel availability at the membrane and assign a putatively novel role for βarrs in regulating canonical effectors for G protein-coupled receptors.
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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.