ArticleJournal of cell science2012
Acute depletion of plasma membrane phosphatidylinositol 4,5-bisphosphate impairs specific steps in endocytosis of the G-protein-coupled receptor.
Article in Journal of cell science, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 53 citations in OpenAlex.
- GPCR Heterodimers: Implications for Biased Signaling.Handbook of experimental pharmacology · 2026Review
- Chemical biology approaches to resolve the subcellular GPCR signaling landscape.Nature chemical biology · 2025Review
- An Irak1-Mecp2 tandem duplication mouse model for the study of MECP2 duplication syndrome.Disease models & mechanisms · 2024Article
- Effect of hormone-induced plasma membrane phosphatidylinositol 4,5-bisphosphate depletion on receptor endocytosis suggests the importance of local regulation in phosphoinositide signaling.Scientific reports · 2024Article
- Nanoscale Phosphoinositide Distribution on Cell Membranes of Mouse Cerebellar Neurons.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2023Article
- Article
- Functional Characterization of the mmBio · 2021Article
- β-arrestin-dependent PI(4,5)PProceedings of the National Academy of Sciences of the United States of America · 2021Article
- TAT-RasGAPProceedings of the National Academy of Sciences of the United States of America · 2020Article
- β-Arrestin-Biased ATJACC. Basic to translational science · 2020Article
- ORP3 phosphorylation regulates phosphatidylinositol 4-phosphate and CaJournal of cell science · 2020Article
- JC Polyomavirus Entry by Clathrin-Mediated Endocytosis Is Driven by β-Arrestin.Journal of virology · 2019Article
- Phosphatidylinositol 4-phosphate is a major source of GPCR-stimulated phosphoinositide production.Science signaling · 2018Article
- Heterologous phosphorylation-induced formation of a stability lock permits regulation of inactive receptors by β-arrestins.The Journal of biological chemistry · 2018Article
- Plasma membrane phosphatidylinositol 4-phosphate and 4,5-bisphosphate determine the distribution and function of K-Ras4B but not H-Ras proteins.The Journal of biological chemistry · 2017Article
- Monitoring G protein-coupled receptor and β-arrestin trafficking in live cells using enhanced bystander BRET.Nature communications · 2016Article
- Valproic Acid Influences MTNR1A Intracellular Trafficking and Signaling in a β-Arrestin 2-Dependent Manner.Molecular neurobiology · 2016Article
- BRET-monitoring of the dynamic changes of inositol lipid pools in living cells reveals a PKC-dependent PtdIns4P increase upon EGF and M3 receptor activation.Biochimica et biophysica acta · 2016Article
- Guidelines for the Use of Protein Domains in Acidic Phospholipid Imaging.Methods in molecular biology (Clifton, N.J.) · 2016Review
- Mutation in the V2 vasopressin receptor gene, AVPR2, causes nephrogenic syndrome of inappropriate diuresis.Kidney international · 2015Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
Abstract
Receptor endocytosis plays an important role in regulating the responsiveness of cells to specific ligands. Phosphatidylinositol 4,5-bisphosphate [PtdIns(4,5)P(2)] has been shown to be crucial for endocytosis of some cell surface receptors, such as EGF and transferrin receptors, but its role in G-protein-coupled receptor internalization has not been investigated. By using luciferase-labeled type 1 angiotensin II (AT1R), type 2C serotonin (5HT2CR) or β(2) adrenergic (β2AR) receptors and fluorescently tagged proteins (β-arrestin-2, plasma-membrane-targeted Venus, Rab5) we were able to follow the sequence of molecular interactions along the endocytic route of the receptors in HEK293 cells using the highly sensitive method of bioluminescence resonance energy transfer and confocal microscopy. To study the role of plasma membrane PtdIns(4,5)P(2) in receptor endocytosis, we used our previously developed rapamycin-inducible heterodimerization system, in which the recruitment of a 5-phosphatase domain to the plasma membrane degrades PtdIns(4,5)P(2). Here we show that ligand-induced interaction of AT1, 5HT2C and β(2)A receptors with β-arrestin-2 was unaffected by PtdIns(4,5)P(2) depletion. However, trafficking of the receptors to Rab5-positive early endosomes was completely abolished in the absence of PtdIns(4,5)P(2). Remarkably, removal of the receptors from the plasma membrane was reduced but not eliminated after PtdIns(4,5)P(2) depletion. Under these conditions, stimulated AT1 receptors clustered along the plasma membrane, but did not enter the cells. Our data suggest that in the absence of PtdIns(4,5)P(2), these receptors move into clathrin-coated membrane structures, but these are not cleaved efficiently and hence cannot reach the early endosomal compartment.
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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.