ArticleBMC neuroscience2014
Nanoscopic spine localization of Norbin, an mGluR5 accessory protein.
Article in BMC neuroscience, 2014. 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, 28 citations in OpenAlex.
- Temporal and protein-specific S-palmitoylation supports synaptic and neural network plasticity.Cellular and molecular life sciences : CMLS · 2025Article
- Spontaneous glutamate release activates mGluR signaling to drive rapid antidepressant responses.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Postsynaptic Density Proteins and Their Role in the Trafficking of Group I Metabotropic Glutamate Receptors.The Journal of membrane biology · 2024Review
- Super-resolution imaging reveals nucleolar encapsulation by single-stranded DNA.Journal of cell science · 2024Article
- Functions and mechanisms of the GPCR adaptor protein Norbin.Biochemical Society transactions · 2023Review
- Article
- mGluR5 is transiently confined in perisynaptic nanodomains to shape synaptic function.Nature communications · 2023Article
- Functional organization of postsynaptic glutamate receptors.Molecular and cellular neurosciences · 2018Review
- Altered Norbin Expression in Patients with Epilepsy and a Rat Model.Scientific reports · 2017Article
- Article
- Super resolution microscopy is poised to reveal new insights into the formation and maturation of dendritic spines.F1000Research · 2016Review
- Focusing super resolution on the cytoskeleton.F1000Research · 2016Review
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundNorbin is a neuron-specific, cytosolic protein that interacts with the metabotropic glutamate receptor 5 (mGluR5) and has a profound impact on mGluR5 signaling. Yet, little is known about its synaptic distribution.
resultsHere we have analyzed the spatial relationship between Norbin, postsynaptic density protein 95 (PSD-95), actin and mGluR5 in spines using super-resolution microscopy. Norbin was found to have a high degree of colocalization with actin and a lower degree of colocalization with PSD-95. Co-immunoprecipitation studies confirmed that interaction occurs between Norbin and actin, but not between Norbin and PSD-95. Norbin was also found to have a high degree of colocalization with the perisynaptically located mGluR5. Findings based on structured illumination microscopy (3D-SIM) of exogenous expressed Norbin-GFP were confirmed by stimulated emission depletion microscopy (STED) of immunolabeled endogenous Norbin.
conclusionsNorbin associates with actin rather than with PSD-95 in dendritic spines. Results regarding protein localization and colocalization performed with conventional confocal microscopy must be interpreted with great caution. The now available super-resolution microscopy techniques provide more accurate information about sub-cellular protein localization than previously was possible.
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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.