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The Journal of Neuroscience, January 1, 1998, 18(1):128-137

Interaction of Muscle and Brain Sodium Channels with Multiple Members of the Syntrophin Family of Dystrophin-Associated Proteins

Stephen H. Gee1, Raghavan Madhavan1, S. Rock Levinson2, John H. Caldwell2, Robert Sealock1, and Stanley C. Froehner1

1 Department of Physiology, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina, 27599-7545, and 2 Department of Cellular and Structural Biology, Department of Physiology and the Neuroscience Program, University of Colorado Health Sciences Center, Denver, Colorado 80262

Syntrophins are cytoplasmic peripheral membrane proteins of the dystrophin-associated protein complex (DAPC). Three syntrophin isoforms, alpha 1, beta 1, and beta 2, are encoded by distinct genes. Each contains two pleckstrin homology (PH) domains, a syntrophin-unique (SU) domain, and a PDZ domain. The name PDZ comes from the first three proteins found to contain repeats of this domain (PSD-95, Drosophila discs large protein, and the zona occludens protein 1). PDZ domains in other proteins bind to the C termini of ion channels and neurotransmitter receptors containing the consensus sequence (S/T)XV-COOH and mediate the clustering or synaptic localization of these proteins. Two voltage-gated sodium channels (NaChs), SkM1 and SkM2, of skeletal and cardiac muscle, respectively, have this consensus sequence. Because NaChs are sarcolemmal components like syntrophins, we have investigated possible interactions between these proteins. NaChs copurify with syntrophin and dystrophin from extracts of skeletal and cardiac muscle. Peptides corresponding to the C-terminal 10 amino acids of SkM1 and SkM2 are sufficient to bind detergent-solubilized muscle syntrophins, to inhibit the binding of native NaChs to syntrophin PDZ domain fusion proteins, and to bind specifically to PDZ domains from alpha 1-, beta 1-, and beta 2-syntrophin. These peptides also inhibit binding of the syntrophin PDZ domain to the PDZ domain of neuronal nitric oxide synthase, an interaction that is not mediated by C-terminal sequences. Brain NaChs, which lack the (S/T)XV consensus sequence, also copurify with syntrophin and dystrophin, an interaction that does not appear to be mediated by the PDZ domain of syntrophin. Collectively, our data suggest that syntrophins link NaChs to the actin cytoskeleton and the extracellular matrix via dystrophin and the DAPC.

Key words: syntrophin; dystrophin complex; PDZ domain; PH domain; neuromuscular junction; sodium channel; cytoskeleton; surface plasmon resonance

Copyright © 1998 Society for Neuroscience  0270-6474/98/181128-10$05.00/0


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