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First published online November 3, 2003
doi: 10.1242/10.1242/jcs.00805

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ß-Dystrobrevin interacts directly with kinesin heavy chain in brain

Laboratory of Cell Biology, Istituto Superiore di Sanità, Viale Regina Elena 299, 00161 Rome, Italy

^* Author for correspondence (e-mail: macioce{at}iss.it)

Accepted 28 July 2003

ß-Dystrobrevin, a member of the dystrobrevin protein family, is a dystrophin-related and -associated protein restricted to non-muscle tissues and is highly expressed in kidney, liver and brain. Dystrobrevins are now thought to play an important role in intracellular signal transduction, in addition to providing a membrane scaffold in muscle, but the precise role of ß-dystrobrevin has not yet been determined. To study ß-dystrobrevin's function in brain, we used the yeast two-hybrid approach to look for interacting proteins. Four overlapping clones were identified that encoded Kif5A, a neuronal member of the Kif5 family of proteins that consists of the heavy chains of conventional kinesin. A direct interaction of ß-dystrobrevin with Kif5A was confirmed by in vitro and in vivo association assays. Co-immunoprecipitation with a monoclonal kinesin heavy chain antibody precipitated both - and ß-dystrobrevin, indicating that this interaction is not restricted to the ß-dystrobrevin isoform. The site for Kif5A binding to ß-dystrobrevin was localized in a carboxyl-terminal region that seems to be important in heavy chain-mediated kinesin interactions and is highly homologous in all three Kif5 isoforms, Kif5A, Kif5B and Kif5C. Pull-down and immunofluorescence experiments also showed a direct interaction between ß-dystrobrevin and Kif5B. Our findings suggest a novel function for dystrobrevin as a motor protein receptor that might play a major role in the transport of components of the dystrophin-associated protein complex to specific sites in the cell.

Key words: Dystrobrevin, Kinesin, Yeast two-hybrid, Brain, Dystroglycan

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