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Published online 2 October 2000. doi:10.1083/jcb.151.1.53
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© The Rockefeller University Press, 0021-9525/2000//53 $5.00
The Journal of Cell Biology, Volume 151, Number 1, , 2000 53-68

Original Article

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



Iryna M. Ethella, Kazuki Hagiharaa, Yoshiaki Miuraa, Fumitoshi Iriea, and Yu Yamaguchia

a The Burnham Institute, La Jolla, California 92037
The Burnham Institute, 10901 North Torrey Pines Road, La Jolla, CA 92037.(858) 646-3199(858) 646-3124

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.

Key Words: heparan sulfate proteoglycan • dendritic spines • spine apparatus • synapse • vesicle transport

© 2000 The Rockefeller University Press

Abbreviations used in this paper: CNS, central nervous system; DIV, days in vitro; E, embryonic day; GFP, green fluorescent protein; GRIP, glutamate receptor–interacting protein; GST, glutathione-S-transferase; His, hexahistidine; HSPG, heparan sulfate proteoglycan; PSD, postsynaptic density; RT, reverse transcriptase; RyR-2, ryanodine receptor; SNARE, soluble NSF attachment protein receptor; TRAPP, transport protein particle.


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