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Ankyrin and spectrin associate with voltage-dependent sodium channels in brain

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Abstract

The segregation of voltage-dependent sodium channels to specialized regions of the neuron is crucial for propagation of an action potential1–5. Studies of their lateral mobility indicate that sodium channels are freely mobile on the neuronal cell body but are immobile at the axon hillock, presynaptic terminal and at focal points along the axon6. To elucidate the mechanisms that regulate sodium channel topography and mobility, we searched for specific proteins from the brain that associate with sodium channels. Here we show that sodium channels labelled with 3H-saxitoxin (STX) are precipitated in the presence of exogenous brain ankyrin by anti-ankyrin antibodies and that 125I-labelled ankyrin binds with high affinity to sodium channels reconstituted into lipid vesicles. The cytoplasmic domain of the erythrocyte anion transporter competes for the latter interaction. Neither the neuronal GAB A (γ-aminobutyric acid) receptor channel complex nor the dihy-dropyridine (DHP) receptor bind brain ankyrin. The results indicate that brain ankyrin links the voltage-dependent sodium channel to the underlying cytoskeleton and may help to maintain axolem-mal membrane heterogeneity and control sodium channel mobility.

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Author notes

  1. Kimon Angelides: To whom correspondence should be addressed.

Authors and Affiliations

  1. Department of Physiology and Molecular Biophysics, Baylor College of Medicine, Houston, Texas, 77030, USA

    Yogambal Srinivasan, Lawrence Elmer & Kimon Angelides

  2. The Howard Hughes Medical Institute and the Department of Biochemistry, Duke University Medical Center, Durham, North Carolina, 27710, USA

    Jonathan Davis & Vann Bennett

Authors
  1. Yogambal Srinivasan
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  2. Lawrence Elmer
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  3. Jonathan Davis
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  4. Vann Bennett
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  5. Kimon Angelides
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Srinivasan, Y., Elmer, L., Davis, J. et al. Ankyrin and spectrin associate with voltage-dependent sodium channels in brain. Nature 333, 177–180 (1988). https://doi.org/10.1038/333177a0

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  • DOI: https://doi.org/10.1038/333177a0

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