Synbindin, a Novel Syndecan-2–Binding Protein in Neuronal Dendritic Spines

Dendritic spines are small protrusions on the surface of dendrites that receive the vast majority of excitatory synapses. We previously showed that the cell-surface heparan sulfate proteoglycan syndecan-2 induces spine formation upon transfection into hippocampal neurons. This effect requires the CO...

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Main Authors:	Ethell, Iryna M., Hagihara, Kazuki, Miura, Yoshiaki, Irie, Fumitoshi, Yamaguchi, Yu
Format:	Online
Language:	English
Published:	The Rockefeller University Press 2000
Online Access:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2189810/

id	pubmed-2189810
recordtype	oai_dc
spelling	pubmed-21898102008-05-01 Synbindin, a Novel Syndecan-2–Binding Protein in Neuronal Dendritic Spines Ethell, Iryna M. Hagihara, Kazuki Miura, Yoshiaki Irie, Fumitoshi Yamaguchi, Yu Original Article Dendritic spines are small protrusions on the surface of dendrites that receive the vast majority of excitatory synapses. We previously showed that the cell-surface heparan sulfate proteoglycan syndecan-2 induces spine formation upon transfection into hippocampal neurons. This effect requires the COOH-terminal EFYA sequence of syndecan-2, suggesting that cytoplasmic molecules interacting with this sequence play a critical role in spine morphogenesis. Here, we report a novel protein that binds to the EFYA motif of syndecan-2. This protein, named synbindin, is expressed by neurons in a pattern similar to that of syndecan-2, and colocalizes with syndecan-2 in the spines of cultured hippocampal neurons. In transfected hippocampal neurons, synbindin undergoes syndecan-2–dependent clustering. Synbindin is structurally related to yeast proteins known to be involved in vesicle transport. Immunoelectron microscopy localized synbindin on postsynaptic membranes and intracellular vesicles within dendrites, suggesting a role in postsynaptic membrane trafficking. Synbindin coimmunoprecipitates with syndecan-2 from synaptic membrane fractions. Our results show that synbindin is a physiological syndecan-2 ligand on dendritic spines. We suggest that syndecan-2 induces spine formation by recruiting intracellular vesicles toward postsynaptic sites through the interaction with synbindin. The Rockefeller University Press 2000-10-02 /pmc/articles/PMC2189810/ /pubmed/11018053 Text en © 2000 The Rockefeller University Press This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).
repository_type	Open Access Journal
institution_category	Foreign Institution
institution	US National Center for Biotechnology Information
building	NCBI PubMed
collection	Online Access
language	English
format	Online
author	Ethell, Iryna M. Hagihara, Kazuki Miura, Yoshiaki Irie, Fumitoshi Yamaguchi, Yu
spellingShingle	Ethell, Iryna M. Hagihara, Kazuki Miura, Yoshiaki Irie, Fumitoshi Yamaguchi, Yu Synbindin, a Novel Syndecan-2–Binding Protein in Neuronal Dendritic Spines
author_facet	Ethell, Iryna M. Hagihara, Kazuki Miura, Yoshiaki Irie, Fumitoshi Yamaguchi, Yu
author_sort	Ethell, Iryna M.
title	Synbindin, a Novel Syndecan-2–Binding Protein in Neuronal Dendritic Spines
title_short	Synbindin, a Novel Syndecan-2–Binding Protein in Neuronal Dendritic Spines
title_full	Synbindin, a Novel Syndecan-2–Binding Protein in Neuronal Dendritic Spines
title_fullStr	Synbindin, a Novel Syndecan-2–Binding Protein in Neuronal Dendritic Spines
title_full_unstemmed	Synbindin, a Novel Syndecan-2–Binding Protein in Neuronal Dendritic Spines
title_sort	synbindin, a novel syndecan-2–binding protein in neuronal dendritic spines
description	Dendritic spines are small protrusions on the surface of dendrites that receive the vast majority of excitatory synapses. We previously showed that the cell-surface heparan sulfate proteoglycan syndecan-2 induces spine formation upon transfection into hippocampal neurons. This effect requires the COOH-terminal EFYA sequence of syndecan-2, suggesting that cytoplasmic molecules interacting with this sequence play a critical role in spine morphogenesis. Here, we report a novel protein that binds to the EFYA motif of syndecan-2. This protein, named synbindin, is expressed by neurons in a pattern similar to that of syndecan-2, and colocalizes with syndecan-2 in the spines of cultured hippocampal neurons. In transfected hippocampal neurons, synbindin undergoes syndecan-2–dependent clustering. Synbindin is structurally related to yeast proteins known to be involved in vesicle transport. Immunoelectron microscopy localized synbindin on postsynaptic membranes and intracellular vesicles within dendrites, suggesting a role in postsynaptic membrane trafficking. Synbindin coimmunoprecipitates with syndecan-2 from synaptic membrane fractions. Our results show that synbindin is a physiological syndecan-2 ligand on dendritic spines. We suggest that syndecan-2 induces spine formation by recruiting intracellular vesicles toward postsynaptic sites through the interaction with synbindin.
publisher	The Rockefeller University Press
publishDate	2000
url	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2189810/
_version_	1611429080408784896

Synbindin, a Novel Syndecan-2–Binding Protein in Neuronal Dendritic Spines

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