gamma-Syntrophin scaffolding is spatially and functionally distinct from that of the alpha/beta syntrophins.

The syntrophins are a family of scaffolding proteins with multiple protein interaction domains that link signaling proteins to dystrophin family members. Each of the three most characterized syntrophins (alpha, beta1, beta2) contains a PDZ domain that binds a unique set of signaling proteins including kinases, ion and water channels, and ...
neuronal nitric oxide synthase (nNOS). The PDZ domains of the gamma-syntrophins do not bind nNOS. In vitro pull-down assays show that the gamma-syntrophins can bind dystrophin but have unique preferences for the syntrophin binding sites of dystrophin family members. Despite their ability to bind dystrophin in vitro, neither gamma-syntrophin isoform co-localizes with dystrophin in skeletal muscle. Furthermore, gamma-syntrophins do not co-purify with dystrophin isolated from mouse tissue. These data suggest that the interaction of gamma-syntrophin with dystrophin is transient and potentially subject to regulatory mechanisms. gamma1-Syntrophin is highly expressed in brain and is specifically localized in hippocampal pyramidal neurons, Purkinje neurons in cerebellum, and cortical neurons. gamma2-Syntrophin is expressed in many tissues including skeletal muscle where it is found only in the subsynaptic space beneath the neuromuscular junction. In both neurons and muscle, gamma-syntrophin isoforms localize to the endoplasmic reticulum where they may form a scaffold for signaling and trafficking.
Mesh Terms:
Amino Acid Sequence, Animals, Antibodies, Dystrophin, Dystrophin-Associated Proteins, Gene Expression Profiling, Humans, Mice, Molecular Sequence Data, Neurons, Nitric Oxide Synthase Type I, Protein Binding, Protein Isoforms, Protein Structure, Tertiary, Protein Transport, Purkinje Cells, Sarcoplasmic Reticulum, Sequence Homology, Amino Acid
Exp. Cell Res.
Date: Oct. 01, 2006
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