EphB/syndecan-2 signaling in dendritic spine morphogenesis
Open accessAbstract
We previously reported that the cell surface proteoglycan syndecan-2 can induce dendritic spine formation in hippocampal neurons. We demonstrate here that the EphB2 receptor tyrosine kinase phosphorylates syndecan-2 and that this phosphorylation event is crucial for syndecan-2 clustering and spine formation. Syndecan-2 is tyrosine phosphorylated and forms a complex with EphB2 in mouse brain. Dominant-negative inhibition of endogenous EphB receptor activities blocks clustering of endogenous syndecan-2 and normal spine formation in cultured hippocampal neurons. This is the first evidence that Eph receptors play a physiological role in dendritic spine morphogenesis. Our observations suggest that spine morphogenesis is triggered by the activation of Eph receptors, which causes tyrosine phosphorylation of target molecules, such as syndecan-2, in presumptive spines.
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Activation of EphB2 receptor tyrosine kinase and the subsequent interaction of syndecan-2 with PDZ domain proteins, such as syntenin and calcium/calmodulin-dependent serine protein kinase, appear to relay the extracellular signals to the intracellular cytoskeleton/signaling complex.
“Activation of EphB2 receptor tyrosine kinase and the subsequent interaction of syndecan-2 with PDZ domain proteins, such as syntenin and calcium/calmodulin-dependent serine protein kinase, appear to relay the extracellular signals to the intracellular cytoskeleton/signaling complex (Ethell et al., 2001).”
From Apolipoprotein E in Synaptic Plasticity and Alzheimer’s Disease: Potential Cellular and Molecular Mechanisms (2014) · cites this paper as Ethell et al., 2001
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- Authors
- Ethell, I. M., Irie, F., Kalo, M. S., Couchman, J. R., Pasquale, E. B., & Yamaguchi, Y.
- Affiliations
- Sanford Burnham Prebys Medical Discovery Institute (US)
- University of Alabama at Birmingham (US)
- Corresponding author
- Yamaguchi, Yu
- Venue
- Neuron
- Publisher
- Elsevier BV
- Published
- 2001-09
- Volume
- 31
- Issue
- 6
- Pages
- 1001-1013
- ISSN
- 0896-6273 (ISSN-L)
- OpenAlex
- W2091334133
- Cited by
- 309
- References
- 3
- Citations by year
- 2026: 2 · 2025: 2 · 2024: 3 · 2023: 4 · 2022: 2 · 2021: 6 · 2020: 6 · 2019: 5 · 2018: 13 · 2017: 3 · 2016: 9 · 2015: 13 · 2014: 14 · 2013: 11 · 2012: 12
- FWCI
- 9.57
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Neuron (publishedVersion)
- PubMed (publishedVersion)
- Research at the University of Copenhagen (University of Copenhagen) (submittedVersion)
- Funders
- National Institute of General Medical Sciences (R01GM050194, GM50194)
- Eunice Kennedy Shriver National Institute of Child Health and Human Development (HD 25938, P01HD025938)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Axon Guidance and Neuronal Signaling
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Proteoglycans and glycosaminoglycans research
- Keywords
- EphB2, syndecan-2, dendritic spine morphogenesis, receptor tyrosine kinase, tyrosine phosphorylation, hippocampal neurons, synaptic development
- MeSH terms
- Animals, Cells, Cultured, Dendrites, Hippocampus, Membrane Glycoproteins, Morphogenesis, Nerve Tissue Proteins, Neuronal Plasticity, Phosphorylation, Protein Processing, Post-Translational, Proteoglycans, Transfection, Signal Transduction, Mutagenesis, Site-Directed, Phosphotyrosine, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Excitatory Postsynaptic Potentials, Receptor Protein-Tyrosine Kinases, Receptor, EphB2, Mice, Rats, Syndecan-2
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