Evidence map›Paper›PMID 10725395›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2000

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

R A Garcia, K Vasudevan, A Buonanno

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 111 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
111citing papers in PubMed, 1 pooled it
6.9field-weighted citation impact, top 2% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

111 citing papers in PubMed, 1 synthesis or guideline pooled it, 266 citations in OpenAlex.

  1. Pooled it
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  14. Review
  15. PSD95: A synaptic protein implicated in schizophrenia or autism?Progress in neuro-psychopharmacology & biological psychiatry · 2018
    Review
  16. Altered expression of schizophrenia-related genes in mice lacking mGlu5 receptors.European archives of psychiatry and clinical neuroscience · 2018
    Article
  17. Structural Similarities between Neuregulin 1-3 Isoforms Determine Their Subcellular Distribution and Signaling Mode in Central Neurons.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2017
    Article
  18. Review
  19. Article
  20. Review

51 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

R A GarciaUnit on Molecular Neurobiology, National Institutes of Health, Bethesda, MD 20892, USA.
K Vasudevan
A Buonanno
National Institutes of Health · US

Funding

Neuregulin-ErbB Signaling in Neuronal Development and Psychiatric DisordersZIAHD000711 · NICHD · EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH & HUMAN DEVELOPMENT · PI BUONANNO, ANDRES · 2009 to 2024
$24.4M
TRANSCRIPTION REGULATION OF SYNAPSE-SPECIFIC GENES IN SKELETAL MUSCLEZ01HD000711 · NICHD · EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH & HUMAN DEVELOPMENT · PI BUONANNO, ANDRES · 1990 to 2008
$2.4M
6 · The paper itself

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 beta(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.

Indexed as

AnimalsBase SequenceCells, CulturedDNA PrimersErbB ReceptorsGuanylate KinasesHippocampusImmunohistochemistryNerve Tissue ProteinsNeuronsProtein BindingRatsRats, Sprague-DawleyReceptor, ErbB-4SAP90-PSD95 Associated ProteinsSynapsesDLG2 protein, humanDNA PrimersERBB4 protein, humanErbb4 protein, ratErbB ReceptorsGuanylate KinasesNerve Tissue ProteinsReceptor, ErbB-4SAP90-PSD95 Associated ProteinsTumor Suppressor Proteins

Identifiers

PMID10725395
PMCPMC16285
OpenAlexW2061684042

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.