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

@article{citeulike:1697283, abstract = {The segregation of voltage-dependent sodium channels to specialized regions of the neuron is crucial for propagation of an action potential. 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 axon. 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 GABA (gamma-aminobutyric acid) receptor channel complex nor the dihydropyridine (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 axolemmal membrane heterogeneity and control sodium channel mobility.}, address = {Department of Physiology and Molecular Biophysics, Baylor College of Medicine, Houston, Texas 77030.}, author = {Srinivasan, Y. and Elmer, L. and Davis, J. and Bennett, V. and Angelides, K.}, citeulike-article-id = {1697283}, citeulike-linkout-0 = {http://dx.doi.org/10.1038/333177a0}, citeulike-linkout-1 = {http://view.ncbi.nlm.nih.gov/pubmed/2452986}, citeulike-linkout-2 = {http://www.hubmed.org/display.cgi?uids=2452986}, doi = {10.1038/333177a0}, issn = {0028-0836}, journal = {Nature}, month = {May}, number = {6169}, pages = {177--180}, posted-at = {2007-09-26 14:27:37}, priority = {0}, title = {Ankyrin and spectrin associate with voltage-dependent sodium channels in brain.}, url = {http://dx.doi.org/10.1038/333177a0}, volume = {333}, year = {1988} }

TY - JOUR ID - citeulike:1697283 L3 - citeulike-article-id:1697283 N2 - The segregation of voltage-dependent sodium channels to specialized regions of the neuron is crucial for propagation of an action potential. 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 axon. 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 GABA (gamma-aminobutyric acid) receptor channel complex nor the dihydropyridine (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 axolemmal membrane heterogeneity and control sodium channel mobility. IS - 6169 JF - Nature SN - 0028-0836 AD - Department of Physiology and Molecular Biophysics, Baylor College of Medicine, Houston, Texas 77030. EP - 180 TI - Ankyrin and spectrin associate with voltage-dependent sodium channels in brain. VL - 333 SP - 177 AU - Srinivasan, Y AU - Elmer, L AU - Davis, J AU - Bennett, V AU - Angelides, K PY - 1988/05/12/ UR - http://dx.doi.org/10.1038/333177a0 ER -