The DOI matches its Crossref record; 70 of the 70 references it cites were found in a registry or an index.
The neuregulin receptor ErbB-4 interacts with PDZ-containing proteins at neuronal synapses
Open accessAbstract
Neuregulins regulate the expression of ligand- and voltage-gated channels in neurons and skeletal muscle by the activation of their cognate tyrosine kinase receptors, ErbB 1–4. The subcellular distribution and mechanisms that regulate the localization of ErbB receptors are unknown. We have found that ErbB receptors are present in brain subcellular fractions enriched for postsynaptic densities (PSD). The ErbB-4 receptor is unique among the ErbB proteins because its C-terminal tail (T-V-V) conforms to a sequence that binds to a protein motif known as the PDZ domain. Using the yeast two-hybrid system, we found that the C-terminal region of ErbB-4 interacts with the three related membrane-associated guanylate kinases (MAGUKs) PSD-95/SAP90, PSD-93/chapsyn-110, and SAP 102, which harbor three PDZ domains, as well as with β 2 -syntrophin, which has a single PDZ domain. As with N -methyl- d -aspartate (NMDA) receptors, ErbB4 interacts with the first two PDZ domains of PSD-95. Using coimmunoprecipitation assays, we confirmed the direct interactions between ErbB-4 and PSD-95 in transfected heterologous cells, as well as in vivo , where both proteins are coimmunoprecipitated from brain lysates. Moreover, evidence for colocalization of these proteins was also observed by immunofluorescence in cultured hippocampal neurons. ErbB-4 colocalizes with PSD-95 and NMDA receptors at a subset of excitatory synapses apposed to synaptophysin-positive presynaptic terminals. The capacity of ErbB receptors to interact with PDZ-domain proteins at cell junctions is conserved from invertebrates to mammals. As discussed, the interactions found between receptor tyrosine kinases and MAGUKs at neuronal synapses may have important implications for activity-dependent plasticity.
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“Erbb4 is a receptor tyrosine kinase that can interact with postsynaptic density proteins (Garcia et al., 2000).”
From MicroRNA‐138‐5p suppresses excitatory synaptic strength at the cerebellar input layer (2025) · cites this paper as Garcia et al., 2000
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“ErbB4 and DISC1 interact with PSD-95 in spines54,58.”
From Dendritic spine pathology in neuropsychiatric disorders (2011) · cites this paper as [58]
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Dendritic spine pathology in neuropsychiatric disorders
Penzes, P., Cahill, M. E., Jones, K. A., VanLeeuwen, J.-E., & Woolfrey, K. M. (2011) · Nature Neuroscience · doi:10.1038/nn.2741 · Cited by 1,523
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“More recently, Hoon et al. [226] showed NL4 was endogenously localized to inhibitory glycinergic synapses in the retina and other areas of the CNS, associates with gephyrin but not PSD-95 in vivo, and is important for glycinergicdependent inhibitory transmission in the retina.”
BackgroundInfluential
Metadata
- Authors
- Garcia, R. A. G., Vasudevan, K., & Buonanno, A.
- Affiliations
- National Institutes of Health (US)
- Unit on Molecular Neurobiology, National Institutes of Health, Bethesda, MD 20892
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2000-03-21
- Volume
- 97
- Issue
- 7
- Pages
- 3596-3601
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC16285
- OpenAlex
- W2061684042
- Cited by
- 278
- References
- 70
- Citations by year
- 2026: 2 · 2025: 3 · 2024: 2 · 2023: 4 · 2022: 2 · 2021: 4 · 2020: 3 · 2019: 4 · 2018: 3 · 2017: 5 · 2016: 7 · 2015: 12 · 2014: 16 · 2013: 15 · 2012: 8
- FWCI
- 8.00
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Health Sciences › Medicine › Oncology › HER2/EGFR in Cancer Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Genetics and Neurodevelopmental Disorders
- Keywords
- ErbB4, PDZ domain, PSD-95, membrane-associated guanylate kinase, synaptic localization, postsynaptic density, receptor tyrosine kinase, NMDA receptor, hippocampal neurons, synaptic plasticity, protein-protein interaction
- MeSH terms
- SAP90-PSD95 Associated Proteins, Animals, Base Sequence, Cells, Cultured, Hippocampus, Immunohistochemistry, Nerve Tissue Proteins, Neurons, Protein Binding, Synapses, Rats, Sprague-Dawley, DNA Primers, Tumor Suppressor Proteins, Rats, Guanylate Kinases, ErbB Receptors, Receptor, ErbB-4
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