Experiments with vesicles containing N-methyl-D-aspartate (NMDA) receptor 2B (NR2B subunit) show that they are transported along microtubules by KIF17, a neuron-specific molecular motor in neuronal dendrites. Selective transport is accomplished by direct interaction of the KIF17 tail with a PDZ domain of mLin-10 (Mint1/X11), which is a constituent of a large protein complex including mLin-2 (CASK), mLin-7 (MALS/Velis), and the NR2B subunit. This interaction, specific for a neurotransmitter receptor critically important for plasticity in the postsynaptic terminal, may be a regulatory point for synaptic plasticity and neuronal morphogenesis.
| Predicate | Object |
|---|---|
| rdf:type | |
| rdfs:comment |
Experiments with vesicles containing N-methyl-D-aspartate (NMDA) receptor 2B (NR2B subunit) show that they are transported along microtubules by KIF17, a neuron-specific molecular motor in neuronal dendrites. Selective transport is accomplished by direct interaction of the KIF17 tail with a PDZ domain of mLin-10 (Mint1/X11), which is a constituent of a large protein complex including mLin-2 (CASK), mLin-7 (MALS/Velis), and the NR2B subunit. This interaction, specific for a neurotransmitter receptor critically important for plasticity in the postsynaptic terminal, may be a regulatory point for synaptic plasticity and neuronal morphogenesis.
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| skos:exactMatch | |
| uniprot:name |
Science
|
| uniprot:author |
Hirokawa N.,
Nakagawa T.,
Seog D.-H.,
Setou M.
|
| uniprot:date |
2000
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| uniprot:pages |
1796-1802
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| uniprot:title |
Kinesin superfamily motor protein KIF17 and mLin-10 in NMDA receptor-containing vesicle transport.
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| uniprot:volume |
288
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| dc-term:identifier |
doi:10.1126/science.288.5472.1796
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