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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6
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pubmed:dateCreated |
2001-10-2
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pubmed:abstractText |
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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pubmed:grant |
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pubmed:commentsCorrections |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphotyrosine,
http://linkedlifedata.com/resource/pubmed/chemical/Proteoglycans,
http://linkedlifedata.com/resource/pubmed/chemical/Receptor, EphB2,
http://linkedlifedata.com/resource/pubmed/chemical/Receptor Protein-Tyrosine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Sdc2 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Sdc2 protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Syndecan-2
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0896-6273
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
27
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pubmed:volume |
31
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1001-13
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:11580899-Animals,
pubmed-meshheading:11580899-Cells, Cultured,
pubmed-meshheading:11580899-Dendrites,
pubmed-meshheading:11580899-Excitatory Postsynaptic Potentials,
pubmed-meshheading:11580899-Hippocampus,
pubmed-meshheading:11580899-Membrane Glycoproteins,
pubmed-meshheading:11580899-Mice,
pubmed-meshheading:11580899-Morphogenesis,
pubmed-meshheading:11580899-Mutagenesis, Site-Directed,
pubmed-meshheading:11580899-Nerve Tissue Proteins,
pubmed-meshheading:11580899-Neuronal Plasticity,
pubmed-meshheading:11580899-Phosphorylation,
pubmed-meshheading:11580899-Phosphotyrosine,
pubmed-meshheading:11580899-Protein Processing, Post-Translational,
pubmed-meshheading:11580899-Proteoglycans,
pubmed-meshheading:11580899-Rats,
pubmed-meshheading:11580899-Receptor, EphB2,
pubmed-meshheading:11580899-Receptor Protein-Tyrosine Kinases,
pubmed-meshheading:11580899-Signal Transduction,
pubmed-meshheading:11580899-Spectrometry, Mass, Matrix-Assisted Laser...,
pubmed-meshheading:11580899-Syndecan-2,
pubmed-meshheading:11580899-Transfection
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pubmed:year |
2001
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pubmed:articleTitle |
EphB/syndecan-2 signaling in dendritic spine morphogenesis.
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pubmed:affiliation |
The Burnham Institute, 10901 North Torrey Pines Road, La Jolla, CA 92037, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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