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Department of Neuroscience, University of Connecticut Health Center, University of Connecticut, Farmington, CT 06032

Correspondence to Matthew N. Rasband: Rasband{at}uchc.edu

High densities of ion channels at axon initial segments (AISs) and nodes of Ranvier are required for initiation, propagation, and modulation of action potentials in axons. The organization of these membrane domains depends on a specialized cytoskeleton consisting of two submembranous cytoskeletal and scaffolding proteins, ankyrinG (ankG) and ßIV spectrin. However, it is not known which of these proteins is the principal organizer, or if the mechanisms governing formation of the cytoskeleton at the AIS also apply to nodes. We identify a distinct protein domain in ßIV spectrin required for its localization to the AIS, and show that this domain mediates ßIV spectrin's interaction with ankG. Dominant-negative ankG disrupts ßIV spectrin localization, but does not alter endogenous ankG or Na⁺ channel clustering at the AIS. Finally, using adenovirus for transgene delivery into myelinated neurons, we demonstrate that ßIV spectrin recruitment to nodes of Ranvier also depends on binding to ankG.

Abbreviations used in this paper: AIS, axon initial segment; CAM, cell adhesion molecule; CNS, central nervous system; DIV, days in vitro; DRG, dorsal root ganglion; E, embryonic day; PNS, peripheral nervous system; RGC, retinal ganglion cell.

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