SybindinSybindin-like family |
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| SMART accession number: | SM01399
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| Description: |
Sybindin is a physiological syndecan-2 ligand on dendritic spines, the small protrusions on the surface of dendrites that receive the vast majority of excitatory synapses PMID:11018053. |
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| Interpro abstract (IPR007233): |
This entry includes a group of trafficking protein particle complex subunit (TRAPPC) proteins, such as TPPC1/4 from humans and Trs23/Bet5 from yeasts. Budding yeast Trs23 and Bet5 are components of the TRAPP I, TRAPP II and TRAPP III. TRAPP complexes are guanine nucleotide exchange factors (GEF) for the GTPase Ypt1. TRAPP I plays a key role in the late stages of endoplasmic reticulum to Golgi traffic. RAPP II plays a role in intra-Golgi transport. TRAPP III plays a role in autophagosome formation [ (PUBMED:11239471) (PUBMED:20972447) (PUBMED:20375281) ].
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| GO process: | vesicle-mediated transport (GO:0016192) |
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| GO component: | TRAPP complex (GO:0030008) |
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| Family alignment: |
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There are 0 Sybindin domains in 0 proteins in SMART's nrdb database.
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Literature (relevant references for this domain)
Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.
- Ethell IM, Hagihara K, Miura Y, Irie F, Yamaguchi Y
- Synbindin, A novel syndecan-2-binding protein in neuronal dendritic spines.
- J Cell Biol. 2000; 151: 53-68
- Display abstract
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.
Structure (3D structures containing this domain)3D Structures of Sybindin domains in PDB
| PDB code | Main view | Title | | 2j3t |  | The crystal structure of the bet3-trs33-bet5-trs23 complex. |
| 2zmv |  | Crystal structure of Synbindin |
| 3cue |  | Crystal structure of a TRAPP subassembly activating the Rab Ypt1p |
Links (links to other resources describing this domain)
