ArticlePloS one2013
PDZ domain-mediated interactions of G protein-coupled receptors with postsynaptic density protein 95: quantitative characterization of interactions.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Neuropeptide Y YNaunyn-Schmiedeberg's archives of pharmacology · 2026Article
- Article
- Beneath the surface: endosomal GPCR signaling.Trends in biochemical sciences · 2024Review
- Repeated oxytocin prevents central sensitization by regulating synaptic plasticity via oxytocin receptor in a chronic migraine mouse model.The journal of headache and pain · 2021Article
- International Union of Basic and Clinical Pharmacology. CX. Classification of Receptors for 5-hydroxytryptamine; Pharmacology and Function.Pharmacological reviews · 2021Review
- Regulation of G protein-coupled receptor signaling by plasma membrane organization and endocytosis.Traffic (Copenhagen, Denmark) · 2019Review
- Mechanisms of PDZ domain scaffold assembly illuminated by use of supported cell membrane sheets.eLife · 2019Article
- NR2B-Tyr phosphorylation regulates synaptic plasticity in central sensitization in a chronic migraine rat model.The journal of headache and pain · 2018Article
- A surface plasmon resonance-based method for monitoring interactions between G protein-coupled receptors and interacting proteins.Journal of biological methods · 2016Article
- Structural basis of arc binding to synaptic proteins: implications for cognitive disease.Neuron · 2015Article
- Neuronal expression of the human neuropeptide S receptor NPSR1 identifies NPS-induced calcium signaling pathways.PloS one · 2015Article
- Corticotropin-Releasing Hormone Receptor Type 1 (CRHR1) Clustering with MAGUKs Is Mediated via Its C-Terminal PDZ Binding Motif.PloS one · 2015Article
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10 authors.
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Abstract
G protein-coupled receptors (GPCRs) constitute the largest family of membrane proteins in the human genome. Their signaling is regulated by scaffold proteins containing PDZ domains, but although these interactions are important for GPCR function, they are still poorly understood. We here present a quantitative characterization of the kinetics and affinity of interactions between GPCRs and one of the best characterized PDZ scaffold proteins, postsynaptic density protein 95 (PSD-95), using fluorescence polarization (FP) and surface plasmon resonance (SPR). By comparing these in vitro findings with colocalization of the full-length proteins in cells and with previous studies, we suggest that the range of relevant interactions might extend to interactions with K i = 450 µM in the in vitro assays. Within this range, we identify novel PSD-95 interactions with the chemokine receptor CXCR2, the neuropeptide Y receptor Y2, and four of the somatostatin receptors (SSTRs). The interaction with SSTR1 was further investigated in mouse hippocampal neurons, where we found a clear colocalization between the endogenously expressed proteins, indicating a potential for further investigation of the role of this interaction. The approach can easily be transferred to other receptors and scaffold proteins and this could help accelerate the discovery and quantitative characterization of GPCR-PDZ interactions.
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