ArticleThe Biochemical journal2013
The Arf GAP AGAP2 interacts with β-arrestin2 and regulates β2-adrenergic receptor recycling and ERK activation.
Article in The Biochemical journal, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 15 citations in OpenAlex.
- Immune System and Neuroinflammation in Idiopathic Parkinson's Disease: Association Analysis of Genetic Variants and miRNAs Interactions.Frontiers in genetics · 2021Article
- AGAP2: Modulating TGFβ1-Signaling in the Regulation of Liver Fibrosis.International journal of molecular sciences · 2020Review
- Article
- Arf GAPs and molecular motors.Small GTPases · 2019Review
- Synaptic GAP and GEF Complexes Cluster Proteins Essential for GTP Signaling.Scientific reports · 2017Article
- Direct Functional Interaction of the Kinesin-13 Family Member Kinesin-like Protein 2A (Kif2A) and Arf GAP with GTP-binding Protein-like, Ankyrin Repeats and PH Domains1 (AGAP1).The Journal of biological chemistry · 2016Article
- Regulators and Effectors of Arf GTPases in Neutrophils.Journal of immunology research · 2015Review
- ArfGAPs: key regulators for receptor sorting.Receptors & clinical investigation · 2014Article
- Role of β-arrestins and arrestin domain-containing proteins in G protein-coupled receptor trafficking.Current opinion in cell biology · 2014Review
- Allosteric properties of PH domains in Arf regulatory proteins.Cellular logisticsReview
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
AGAP2 [Arf (ADP-ribosylation factor) GAP (GTPase-activating protein) with GTP-binding-protein-like, ankyrin repeat and PH (pleckstrin homology) domains] is a multidomain Arf GAP that was shown to promote the fast recycling of transferrin receptors. In the present study we tested the hypothesis that AGAP2 regulates the trafficking of β2-adrenergic receptors. We found that AGAP2 formed a complex with β-arrestin1 and β-arrestin2, proteins that are known to regulate β2-adrenergic receptor signalling and trafficking. AGAP2 co-localized with β-arrestin2 on the plasma membrane, and knockdown of AGAP2 expression reduced plasma membrane association of β-arrestin2 upon β2-adrenergic receptor activation. AGAP2 also co-localized with internalized β2-adrenergic receptors on endosomes, and overexpression of AGAP2 slowed accumulation of β2-adrenergic receptor in the perinuclear recycling endosomes. In contrast, knockdown of AGAP2 expression prevented the recycling of the β2-adrenergic receptor back to the plasma membrane. In addition, AGAP2 formed a complex with endogenous ERK (extracellular-signal-regulated kinase) and overexpression of AGAP2 potentiated ERK phosphorylation induced by β2-adrenergic receptors. Taken together, these results support the hypothesis that AGAP2 plays a role in the signalling and recycling of β2-adrenergic receptors.
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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.