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Desmuslin, An Intermediate Filament Protein That Interacts with α-Dystrobrevin and Desmin

Dystrobrevin is a component of the dystrophin-associated protein complex and has been shown to interact directly with dystrophin, α1-syntrophin, and the sarcoglycan complex. The precise role of α-dystrobrevin in skeletal muscle has not yet been determined. To study α-dystrobrevin's function in... Full description

1st Person: Mizuno, Yuji
Additional Persons: Thompson, Terri G.; Guyon, Jeffrey R.; Brosius, Melissa; Imamura, Michihiro; Ozawa, Eijiro; Watkins, Simon C.; Kunkel, Louis M.
Source: in Proceedings of the National Academy of Sciences of the United States of America Vol. 98, No. 11 (2001), p. 6156-6161
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Type of Publication: Article
Language: English
Published: 2001
Keywords: Cell Biology
Online: Volltext
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Summary: Dystrobrevin is a component of the dystrophin-associated protein complex and has been shown to interact directly with dystrophin, α1-syntrophin, and the sarcoglycan complex. The precise role of α-dystrobrevin in skeletal muscle has not yet been determined. To study α-dystrobrevin's function in skeletal muscle, we used the yeast two-hybrid approach to look for interacting proteins. Three overlapping clones were identified that encoded an intermediate filament protein we subsequently named desmuslin (DMN). Sequence analysis revealed that DMN has a short N-terminal domain, a conserved rod domain, and a long C-terminal domain, all common features of type 6 intermediate filament proteins. A positive interaction between DMN and α-dystrobrevin was confirmed with an in vitro coimmunoprecipitation assay. By Northern blot analysis, we find that DMN is expressed mainly in heart and skeletal muscle, although there is some expression in brain. Western blotting detected a 160-kDa protein in heart and skeletal muscle. Immunofluorescent microscopy localizes DMN in a stripe-like pattern in longitudinal sections and in a mosaic pattern in cross sections of skeletal muscle. Electron microscopic analysis shows DMN colocalized with desmin at the Z-lines. Subsequent coimmunoprecipitation experiments confirmed an interaction with desmin. Our findings suggest that DMN may serve as a direct linkage between the extracellular matrix and the Z-discs (through plectin) and may play an important role in maintaining muscle cell integrity.
Item Description: Copyright: Copyright 1993-2001 National Academy of Sciences of the United States of America
Physical Description: Online-Ressource
ISSN: 1091-6490

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