gamma-Syntrophin scaffolding is spatially and functionally distinct from that of the alpha/beta syntrophins.
Exp Cell Res
; 312(16): 3084-95, 2006 Oct 01.
Article
em En
| MEDLINE
| ID: mdl-16857187
ABSTRACT
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.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Proteínas Associadas à Distrofina
Limite:
Animals
/
Humans
Idioma:
En
Revista:
Exp Cell Res
Ano de publicação:
2006
Tipo de documento:
Article
País de afiliação:
Estados Unidos