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First published online November 3, 2003

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Dystrophin delivery

The dystrophin-associated protein complex (DPC) links the actin cytoskeleton to the extracellular matrix in muscle but also functions in non-muscle tissues, such as the kidney and CNS. It comprises several proteins, including dystrophin and dystrobrevin, and mutations in these cause various forms of muscular dystrophy, as well as mental retardation. Pompeo Macioce and co-workers have examined the role of the DPC component ß-dystrobrevin by searching for proteins with which it interacts (see p. 4847). Employing yeast two-hybrid screens, they find that it can interact with KIF5A, a neuronal member of the kinesin family of microtubule-based motor proteins. They then show that both KIF5A and the ubiquitous kinesin heavy chain isoform KIF5B can interact with ß-dystrobrevin in pull-down experiments in vitro and coimmunoprecipitate with it in vivo. Finally, the authors use immunofluorescence analyses to show that KIF5B and ß-dystrobrevin colocalize when expressed in cultured cells. The colocalization pattern resembles a tubulovesicular 'transport network' and disappears when microtubules are disrupted. Macioce and co-workers therefore propose that ß-dystrobrevin acts as an adaptor for kinesin-mediated transport of DPCs along microtubules, which could be important for delivery of the complex to the cell membrane.

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ß-Dystrobrevin interacts directly with kinesin heavy chain in brain

P. Macioce, G. Gambara, M. Bernassola, L. Gaddini, P. Torreri, G. Macchia, C. Ramoni, M. Ceccarini, and T. C. Petrucci
JCS 2003 116: 4847-4856. [Abstract] [Full Text]  

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Related articles in JCS Similar articles in this journal Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Search for Related Content