ArticleMolecular endocrinology (Baltimore, Md.)2008
Regulation of parathyroid hormone type 1 receptor dynamics, traffic, and signaling by the Na+/H+ exchanger regulatory factor-1 in rat osteosarcoma ROS 17/2.8 cells.
Article in Molecular endocrinology (Baltimore, Md.), 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 43 citations in OpenAlex.
- Review
- The Intricacies of Renal Phosphate Reabsorption-An Overview.International journal of molecular sciences · 2024Review
- The molecular sociology of NHERF1 PDZ proteins controlling renal hormone-regulated phosphate transport.Bioscience reports · 2024Article
- Visualization of β-adrenergic receptor dynamics and differential localization in cardiomyocytes.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Probable Potential Role of Urate Transporter Genes in the Development of Metabolic Disorders.Cureus · 2018Review
- Ixazomib enhances parathyroid hormone-induced β-catenin/T-cell factor signaling by dissociating β-catenin from the parathyroid hormone receptor.Molecular biology of the cell · 2017Article
- Origins of PDZ Binding Specificity. A Computational and Experimental Study Using NHERF1 and the Parathyroid Hormone Receptor.Biochemistry · 2017Article
- The PDZ Protein Na+/H+ Exchanger Regulatory Factor-1 (NHERF1) Regulates Planar Cell Polarity and Motile Cilia Organization.PloS one · 2016Article
- Disruption of β-catenin binding to parathyroid hormone (PTH) receptor inhibits PTH-stimulated ERK1/2 activation.Biochemical and biophysical research communications · 2015Article
- Minireview: Role of intracellular scaffolding proteins in the regulation of endocrine G protein-coupled receptor signaling.Molecular endocrinology (Baltimore, Md.) · 2015Review
- International Union of Basic and Clinical Pharmacology. XCIII. The parathyroid hormone receptors--family B G protein-coupled receptors.Pharmacological reviews · 2015Review
- Article
- Article
- Fluorescent ligand-directed co-localization of the parathyroid hormone 1 receptor with the brush-border scaffold complex of the proximal tubule reveals hormone-dependent changes in ezrin immunoreactivity consistent with inactivation.Biochimica et biophysica acta · 2012Article
- NHERF-1 and the regulation of renal phosphate reabsoption: a tale of three hormones.American journal of physiology. Renal physiology · 2012Article
- Arrestin scaffolds NHERF1 to the P2Y12 receptor to regulate receptor internalization.The Journal of biological chemistry · 2012Article
- Structural basis for NHERF1 PDZ domain binding.Biochemistry · 2012Article
- Regulation of GPCR activity, trafficking and localization by GPCR-interacting proteins.British journal of pharmacology · 2012Review
- Roles for NHERF1 and NHERF2 on the regulation of C3a receptor signaling in human mast cells.PloS one · 2012Article
- Regulation of G protein-coupled receptor function by Na+/H+ exchange regulatory factors.Pharmacological reviews · 2011Review
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
The effects of the expression of the Na+/H+ exchanger regulatory factor-1 (NHERF1) on the distribution, dynamics, and signaling properties of the PTH type 1 receptor (PTH1R) were studied in rat osteosarcoma cells ROS 17/2.8. NHERF1 had a dramatic effect on the subcellular distribution of PTH1R, promoting a substantial relocation of the receptor to regions of the plasma membrane located in very close proximity to cytoskeletal fibers. Direct interactions of NHERF1 with the PTH1R and the cytoskeleton were required for these effects, because they were abolished by 1) PTH1R mutations that impair NHERF1 binding, and 2) NHERF1 mutations that impair binding to the PTH1R or the cytoskeleton. NHERF1 reduced significantly the diffusion of the PTH1R by a mechanism that was also dependent on a direct association of NHERF1 with the PTH1R and the cytoskeleton. NHERF1 increased ligand-dependent production of cAMP and induced ligand-dependent rises in intracellular calcium. These effects on calcium were due to increased calcium uptake, as they were blocked by calcium channel inhibitors and by the addition of EGTA to the medium. These calcium effects were abolished by protein kinase A inhibition but phospholipase C inhibition was without effect. Based on these analyses, we propose that, in ROS cells, the presence of NHERF1 induces PTH-dependent calcium signaling by a cAMP-mediated mechanism that involves local protein kinase A-dependent activation of calcium channels.
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