@article{7e3f84c649a2406ebf0677211cf38fa0,
title = "Role for α-dystrobrevin in the pathogenesis of dystrophin-dependent muscular dystrophies",
abstract = "A dystrophin-containing glycoprotein complex (DGC) links the basal lamina surrounding each muscle fibre to the fibre's cytoskeleton, providing both structural support and a scaffold for signalling molecules. Mutations in genes encoding several DGC components disrupt the complex and lead to muscular dystrophy. Here we show that mice deficient in α-dystrobrevin, a cytoplasmic protein of the DGC, exhibit skeletal and cardiac myopathies. Analysis of double and triple mutants indicates that α-dystrobrevin acts largely through the DGC. Structural components of the DGC are retained in the absence of α-dystrobrevin, but a DGC-associated signalling protein, nitric oxide synthase, is displaced from the membrane and nitric-oxide-mediated signalling is impaired. These results indicate that both signalling and structural functions of the DGC are required for muscle stability, and implicate α-dystrobrevin in the former.",
author = "Grady, {R. Mark} and Grange, {Robert W.} and Lau, {Kim S.} and Maimone, {Margaret M.} and Nichol, {Mia C.} and Stull, {James T.} and Sanes, {Joshua R.}",
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year = "1999",
month = aug,
doi = "10.1038/12034",
language = "English (US)",
volume = "1",
pages = "215--220",
journal = "Nature cell biology",
issn = "1465-7392",
publisher = "Nature Publishing Group",
number = "4",
}