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The Journal of Neuroscience, August 18, 2004, 24(33):7230-7240; doi:10.1523/JNEUROSCI.2125-04.2004

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Cellular/Molecular
IV Spectrins Are Essential for Membrane Stability and the Molecular Organization of Nodes of Ranvier

Yang Yang,¹ Sandra Lacas-Gervais,² D. Kent Morest,¹ Michele Solimena,² and Matthew N. Rasband¹

¹Department of Neuroscience, University of Connecticut Health Center, Farmington, Connecticut 06030-3401, and ²Medical School, Technical University Dresden, 01307 Dresden, Germany

High densities of sodium channels at nodes of Ranvier permit action potential conduction and depend on IV spectrins, a family of scaffolding proteins linked to the cortical actin cytoskeleton. To investigate the molecular organization of nodes, we analyzed qv^3J"quivering" mice, whose IV spectrins have a truncated proline-rich "specific" domain (SD) and lack the pleckstrin homology (PH) domain. Central nodes of qv^3J mice, which lack IV spectrins, are significantly broader and have prominent vesicle-filled nodal membrane protrusions, whereas axon shape and neurofilament density are dramatically altered. PNS qv^3J nodes, some with detectable IV spectrins, are less affected. In contrast, a larger truncation of IV spectrins in qv^4J mice, deleting the SD, PH, and ankyrinG binding domains, causes IV spectrins to be undetectable and causes dramatic changes, even in peripheral nodes. These results show that quivering mutations disrupt IV spectrin retention and stability at nodes and that distinct protein domains regulate nodal structural integrity and molecular organization.

Key words: Na⁺ channel; cytoskeleton; axon-glia interaction; myelin; node of Ranvier; axon

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Received June 1, 2004; revised June 28, 2004; accepted June 28, 2004.

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