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Cell surface heparan sulfate proteoglycan syndecan-2 induces the maturation of dendritic spines in rat hippocampal neurons.
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Dendritic spines are small protrusions that receive synapses, and changes in spine morphology are thought to be the structural basis for learning and memory. We demonstrate that the cell surface heparan sulfate proteoglycan syndecan-2 plays a critical role in spine development. Syndecan-2 is concentrated at the synapses, specifically on the dendritic spines of cultured hippocampal neurons, and its accumulation occurs concomitant with the morphological maturation of spines from long thin protrusions to stubby and headed shapes. Early introduction of syndecan-2 cDNA into immature hippocampal neurons, by transient transfection, accelerates spine formation from dendritic protrusions. Deletion of the COOH-terminal EFYA motif of syndecan-2, the binding site for PDZ domain proteins, abrogates the spine-promoting activity of syndecan-2. Syndecan-2 clustering on dendritic protrusions does not require the PDZ domain-binding motif, but another portion of the cytoplasmic domain which includes a protein kinase C phosphorylation site. Our results indicate that syndecan-2 plays a direct role in the development of postsynaptic specialization through its interactions with PDZ domain proteins.
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“Deletion of the C-terminal region of syndecan-2 abrogates the effect of syndecan-2 on spine formation (Ethell and Yamaguchi, 1999).”
From Apolipoprotein E in Synaptic Plasticity and Alzheimer’s Disease: Potential Cellular and Molecular Mechanisms (2014) · cites this paper as Ethell and Yamaguchi, 1999
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Structure and molecular organization of dendritic spines.
Tashiro, A., & Yuste, R. (2003) · PubMed · doi:10.14670/hh-18.617 · Cited by 60
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Metadata
- Authors
- Ethell, I. M., & Yamaguchi, Y.
- Affiliations
- Sanford Burnham Prebys Medical Discovery Institute (US)
- Corresponding author
- Yamaguchi, Yu
- Venue
- The Journal of Cell Biology
- Publisher
- Rockefeller University Press
- Published
- 1999-02-08
- Volume
- 144
- Issue
- 3
- Pages
- 575-586
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- PMC
- PMC2132915
- OpenAlex
- W2139220860
- Cited by
- 209
- References
- 60
- Citations by year
- 2026: 1 · 2024: 1 · 2023: 4 · 2022: 3 · 2021: 7 · 2020: 4 · 2019: 4 · 2018: 4 · 2016: 4 · 2015: 8 · 2014: 12 · 2013: 7 · 2012: 7
- FWCI
- 5.78
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- cc-by-nc-sa
- Locations
- The Journal of Cell Biology (publishedVersion)
- PubMed Central (publishedVersion, cc-by-nc-sa)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (5r01ns033117-04)
- National Institute of Neurological Disorders and Stroke (NS33117)
- Eunice Kennedy Shriver National Institute of Child Health and Human Development (HD 25938, P01HD025938)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Proteoglycans and glycosaminoglycans research
- Life Sciences › Neuroscience › Developmental Neuroscience › Neurogenesis and neuroplasticity mechanisms
- Keywords
- syndecan-2, heparan sulfate proteoglycans, dendritic spine maturation, hippocampal neurons, synaptic development, PDZ domain proteins, protein kinase C phosphorylation, postsynaptic specialization, dendritic protrusions, learning and memory
- MeSH terms
- Amino Acid Sequence, Animals, Base Sequence, Dendrites, Heparitin Sulfate, Heparan Sulfate, Hippocampus, Immunohistochemistry, Membrane Glycoproteins, Neurons, Proteoglycans, Transfection, DNA Primers, DNA, Complementary, Rats, Syndecan-2
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