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The neuregulin receptor ErbB-4 interacts with PDZ-containing proteins at neuronal synapses

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Garcia, Rolando A. G., Vasudevan, Kuzhalini, Buonanno, Andres·2000·Proceedings of the National Academy of Sciences

DOI 10.1073/pnas.97.7.3596PMC PMC16285

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Abstract

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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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
DOI: 10.1073/pnas.97.7.3596
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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The neuregulin receptor ErbB-4 interacts with PDZ-containing proteins at neuronal synapses

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