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      Kinesin superfamily motor protein KIF17 and mLin-10 in NMDA receptor-containing vesicle transport.

      Science (New York, N.Y.)
      Amino Acid Motifs, Amino Acid Sequence, Animals, Binding Sites, Biological Transport, Caenorhabditis elegans Proteins, Cloning, Molecular, Dendrites, metabolism, Dimerization, Kinesin, chemistry, genetics, Male, Membrane Proteins, Mice, Microtubules, Models, Biological, Molecular Motor Proteins, Molecular Sequence Data, Molecular Weight, Organelles, Precipitin Tests, Protein Binding, Proteins, Receptors, N-Methyl-D-Aspartate, Recombinant Proteins, Two-Hybrid System Techniques

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          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.

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