ArticleProceedings of the National Academy of Sciences of the United States of America2012
Engagement of β-arrestin by transactivated insulin-like growth factor receptor is needed for V2 vasopressin receptor-stimulated ERK1/2 activation.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 40 citations in OpenAlex.
- Mu-opioid receptor and receptor tyrosine kinase crosstalk: Implications in mechanisms of opioid tolerance, reduced analgesia to neuropathic pain, dependence, and reward.Frontiers in systems neuroscience · 2022Review
- Functional characterization of a loss-of-function mutant I324M of arginine vasopressin receptor 2 in X-linked nephrogenic diabetes insipidus.Scientific reports · 2021Article
- Transactivation of G protein-coupled receptors (GPCRs) and receptor tyrosine kinases (RTKs): Recent insights using luminescence and fluorescence technologies.Current opinion in endocrine and metabolic research · 2021Review
- Key phosphorylation sites in GPCRs orchestrate the contribution of β-Arrestin 1 in ERK1/2 activation.EMBO reports · 2020Article
- A snake toxin as a theranostic agent for the type 2 vasopressin receptor.Theranostics · 2020Article
- GαNature communications · 2017Article
- Insights into cellular signalling by G protein coupled receptor transactivation of cell surface protein kinase receptors.Journal of cell communication and signaling · 2017Review
- Transactivation of Epidermal Growth Factor Receptor by G Protein-Coupled Receptors: Recent Progress, Challenges and Future Research.International journal of molecular sciences · 2016Review
- Role for engagement of β-arrestin2 by the transactivated EGFR in agonist-specific regulation of δ receptor activation of ERK1/2.British journal of pharmacology · 2015Article
- Receptor sequestration in response to β-arrestin-2 phosphorylation by ERK1/2 governs steady-state levels of GPCR cell-surface expression.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Modulation of cellular signaling by herpesvirus-encoded G protein-coupled receptors.Frontiers in pharmacology · 2015Review
- Cell-surface receptors transactivation mediated by g protein-coupled receptors.International journal of molecular sciences · 2014Review
- Something old, something new and something borrowed: emerging paradigm of insulin-like growth factor type 1 receptor (IGF-1R) signaling regulation.Cellular and molecular life sciences : CMLS · 2014Review
- Vasopressin-2 receptor signaling and autosomal dominant polycystic kidney disease: from bench to bedside and back again.Journal of the American Society of Nephrology : JASN · 2014Review
- An experimental strategy to probe Gq contribution to signal transduction in living cells.The Journal of biological chemistryArticle
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
Abstract
G protein-coupled receptors (GPCRs) have been shown to activate the mitogen-activated protein kinases, ERK1/2, through both G protein-dependent and -independent mechanisms. Here, we describe a G protein-independent mechanism that unravels an unanticipated role for β-arrestins. Stimulation of the V2 vasopressin receptor (V2R) in cultured cells or in vivo in rat kidney medullar collecting ducts led to the activation of ERK1/2 through the metalloproteinase-mediated shedding of a factor activating the insulin-like growth factor receptor (IGFR). This process was found to be both Src- and β-arrestin-dependent. Whereas Src was found to act upstream of the metalloproteinase activation and be required for the release of the IGFR-activating factor, β-arrestins were found to act downstream of the IGFR transactivation. Unexpectedly, the engagement of β-arrestins by the IGFR but not by the V2R was needed to promote the vasopressin-stimulated ERK1/2 activation, indicating that a pool of β-arrestins distinct from those β-arrestins recruited to the V2R acts downstream of the receptor tyrosine kinase to activate ERK1/2. Such a dual site of action for β-arrestins helps explain the pleiotropic actions of this scaffolding protein. Given the role that V2R-stimulated ERK1/2 plays in kidney cell proliferation, this transactivation mechanism may have important implications for renal pathophysiology. Still, the role of β-arrestins downstream of a transactivation event is not limited to the V2R, because we observed a similar involvement for an unrelated GPCR (the platelet-activating factor receptor), indicating that it may be a general mechanism shared among GPCRs.
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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 OpenQuestion graph.