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MBC in Press, published online ahead of print July 6, 2005
Mol. Biol. Cell 10.1091/mbc.E05-02-0112

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Submitted on February 10, 2005
Revised on June 2, 2005
Accepted on June 28, 2005

Specific Interaction of the Actin-binding Domain of Dystrophin with Intermediate Filaments Containing Keratin 19

Michele R. Stone,* Andrea O’Neill, Dawn Catino, and Robert J. Bloch

Department of Physiology, University of Maryland School of Medicine, Baltimore, MD 21201

Monitoring Editor: Guido Guidotti

Cytokeratins 8 and 19 concentrate at costameres of striated muscle and copurify with the dystrophin-glycoprotein complex, perhaps through the interaction of the cytokeratins with the actin-binding domain of dystrophin (Ursitti et al., J. Biol. Chem. 279: 41830-41838, 2004). We overexpressed dystrophin’s actin-binding domain (Dys-ABD), K8 and K19, as well as closely related proteins, in COS-7 cells to assess the basis and specificity of their interaction. Dys-ABD alone associated with actin microfilaments. Expressed with K8 and K19, which form filaments, Dys-ABD associated preferentially with the cytokeratins. This interaction was specific, as the homologous ABD of {beta}I-spectrin failed to interact with K8/K19 filaments, and Dys-ABD did not associate with desmin or K8/K18 filaments. Studies in COS-7 cells and in vitro showed that Dys-ABD binds directly and specifically to K19. Expressed in muscle fibers in vivo, K19 accumulated in the myoplasm in structures that contained dystrophin and spectrin, and disrupted the organization of the sarcolemma. K8 incorporated into sarcomeres, with no effect on the sarcolemma. Our results show that dystrophin interacts through its ABD with K19 specifically, and are consistent with the idea that cytokeratins associate with dystrophin at the sarcolemma of striated muscle.

*Present address: Aeras Global TB Vaccine Foundation, Bethesda, MD, 20814.

Address correspondence to: Robert J. Bloch (rbloch{at}umaryland.edu)




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