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Originally published In Press as doi:10.1074/jbc.M010418200 on April 20, 2001

J. Biol. Chem., Vol. 276, Issue 26, 24232-24241, June 29, 2001
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Dysbindin, a Novel Coiled-coil-containing Protein That Interacts with the Dystrobrevins in Muscle and Brain*

Matthew A. BensonDagger , Sarah E. NeweyDagger §, Enca Martin-Rendon||, Richard Hawkes**, and Derek J. BlakeDagger Dagger Dagger

From the Dagger  Department of Human Anatomy and Genetics, University of Oxford, South Parks Road, Oxford OX1 3QX, United Kingdom, the  Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, United Kingdom, and the ** Department of Cell Biology and Anatomy and Genes and Development Research Group, Faculty of Medicine, University of Calgary Faculty of Medicine, University of Calgary, Calgary, Alberta T2N 4N1, Canada

The dystrophin-associated protein complex (DPC) is required for the maintenance of muscle integrity during the mechanical stresses of contraction and relaxation. In addition to providing a membrane scaffold, members of the DPC such as the alpha -dystrobrevin protein family are thought to play an important role in intracellular signal transduction. To gain additional insights into the function of the DPC, we performed a yeast two-hybrid screen for dystrobrevin-interacting proteins. Here we describe the identification of a dysbindin, a novel dystrobrevin-binding protein. Dysbindin is an evolutionary conserved 40-kDa coiled-coil-containing protein that binds to alpha - and beta -dystrobrevin in muscle and brain. Dystrophin and alpha -dystrobrevin are co-immunoprecipitated with dysbindin, indicating that dysbindin is DPC-associated in muscle. Dysbindin co-localizes with alpha -dystrobrevin at the sarcolemma and is up-regulated in dystrophin-deficient muscle. In the brain, dysbindin is found primarily in axon bundles and especially in certain axon terminals, notably mossy fiber synaptic terminals in the cerebellum and hippocampus. These findings have implications for the molecular pathology of Duchenne muscular dystrophy and may provide an alternative route for anchoring dystrobrevin and the DPC to the muscle membrane.

* This work was supported in part by grants from the Wellcome Trust (to D. J. B.) and the Medical Research Council of Canada (to R. H.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AJ404859.

§ Recipient of a Wellcome Trust Prize studentship.

|| Present address: Oxford BioMedica, Medawar Center, Oxford, OX4 4GA, United Kingdom.

Dagger Dagger Wellcome Trust Senior Fellow. To whom all correspondence should be addressed. Tel./Fax: 44-1865-272183; E-mail: dblake@enterprise.molbiol.ox.ac.uk.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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