Relevant references for this domain

Primary literature for the Sybindin domain is listed below.

Synbindin, A novel syndecan-2-binding protein in neuronal dendritic spines.

Ethell IM, Hagihara K, Miura Y, Irie F, Yamaguchi Y
J Cell Biol. 2000; 151: 53-68

Dendritic spines are small protrusions on the surface of dendrites that receivethe vast majority of excitatory synapses. We previously showed that thecell-surface heparan sulfate proteoglycan syndecan-2 induces spine formation upontransfection into hippocampal neurons. This effect requires the COOH-terminalEFYA sequence of syndecan-2, suggesting that cytoplasmic molecules interactingwith this sequence play a critical role in spine morphogenesis. Here, we report anovel protein that binds to the EFYA motif of syndecan-2. This protein, namedsynbindin, 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. Intransfected hippocampal neurons, synbindin undergoes syndecan-2-dependentclustering. Synbindin is structurally related to yeast proteins known to beinvolved in vesicle transport. Immunoelectron microscopy localized synbindin onpostsynaptic membranes and intracellular vesicles within dendrites, suggesting a role in postsynaptic membrane trafficking. Synbindin coimmunoprecipitates withsyndecan-2 from synaptic membrane fractions. Our results show that synbindin is aphysiological syndecan-2 ligand on dendritic spines. We suggest that syndecan-2induces spine formation by recruiting intracellular vesicles toward postsynaptic sites through the interaction with synbindin.