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

Kinesin superfamily motor protein KIF17 and mLin-10 in NMDA receptor-containing vesicle transport. 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. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Science (New York, N.Y.) Pubmed

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

Science (New York, N.Y.) , Volume 288 (5472): 7 – Jun 29, 2000

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


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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ISSN
0036-8075
DOI
10.1126/science.288.5472.1796
pmid
10846156

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.

Journal

Science (New York, N.Y.)Pubmed

Published: Jun 29, 2000

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