Abstract
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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Motifs
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Amino Acid Sequence
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Animals
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Binding Sites
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Biological Transport
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Caenorhabditis elegans Proteins*
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Cloning, Molecular
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Dendrites / metabolism*
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Dimerization
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Kinesins / chemistry
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Kinesins / genetics
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Kinesins / metabolism*
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Male
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Membrane Proteins*
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Mice
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Microtubules / metabolism
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Models, Biological
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Molecular Motor Proteins / chemistry
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Molecular Motor Proteins / genetics
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Molecular Motor Proteins / metabolism*
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Molecular Sequence Data
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Molecular Weight
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Organelles / metabolism
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Precipitin Tests
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Protein Binding
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Proteins / chemistry
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Proteins / metabolism*
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Receptors, N-Methyl-D-Aspartate / metabolism*
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Recombinant Proteins / chemistry
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Recombinant Proteins / metabolism
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Two-Hybrid System Techniques
Substances
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Caenorhabditis elegans Proteins
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KIF17 protein, mouse
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Membrane Proteins
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Molecular Motor Proteins
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NR2B NMDA receptor
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Proteins
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Receptors, N-Methyl-D-Aspartate
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Recombinant Proteins
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lin-10 protein, C elegans
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Kinesins