@article{c9bc7a30596e11dd8d9f000ea68e967b,
title = "EphB/syndecan-2 signaling in dendritic spine morphogenesis.",
abstract = "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.",
author = "Ethell, {I M} and F Irie and Kalo, {M S} and Couchman, {J R} and Pasquale, {E B} and Y Yamaguchi",
note = "Keywords: Animals; Cells, Cultured; Dendrites; Excitatory Postsynaptic Potentials; Hippocampus; Membrane Glycoproteins; Mice; Morphogenesis; Mutagenesis, Site-Directed; Nerve Tissue Proteins; Neuronal Plasticity; Phosphorylation; Phosphotyrosine; Protein Processing, Post-Translational; Proteoglycans; Rats; Receptor Protein-Tyrosine Kinases; Receptor, EphB2; Signal Transduction; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Syndecan-2; Transfection",
year = "2001",
language = "English",
volume = "31",
pages = "1001--13",
journal = "Neuron",
issn = "0896-6273",
publisher = "Cell Press",
number = "6",
}