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J. Biol. Chem., Vol. 279, Issue 11, 10450-10458, March 12, 2004

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Myospryn Is a Novel Binding Partner for Dysbindin in Muscle^*

Matthew A. Benson, Caroline L. Tinsley, and Derek J. Blake, A Wellcome Trust Senior Fellow in Basic Biomedical Science¶

From the Department of Pharmacology, University of Oxford, Mansfield Road, Oxford, OX1 3QT, United Kingdom

Dysbindin is a coiled-coil-containing protein that was initially identified in a screen for dystrobrevin-interacting proteins. Recently, dysbindin has been shown to be involved in the biogenesis of lysosome-related organelles and is also a major schizophrenia susceptibility factor. Although dysbindin has been implicated in a number of different cellular processes, little is known about its function. To determine the function of dysbindin in muscle, we performed a yeast two-hybrid screen to identify potential interacting proteins. Here we show that dysbindin binds to a novel 413-kDa protein, myospryn, which is expressed in cardiac and skeletal muscle. The transcript encoding myospryn encompasses genethonin-3, a transcript that is down-regulated in muscle from Duchenne muscular dystrophy patients and stretch-responsive protein 553, which is up-regulated in experimental muscle hypertrophy. The C terminus of myospryn contains BBC, FN3, and SPRY domains in a configuration reminiscent of the tripartite motif protein family, as well as the dysbindin-binding site and a region mediating self-association. Dysbindin and myospryn co-immunoprecipitate from muscle extracts and are extensively co-localized. These data demonstrate for the first time that there are tissue-specific ligands for dysbindin that may play important roles in the different disease states involving this protein.

Received for publication, November 19, 2003 , and in revised form, December 19, 2003.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBank^TM/EBI Data Bank with accession number(s) AJ575748.

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

These authors contributed equally to this paper.

Recipient of a Wellcome Trust Prize Studentship.

^¶ To whom correspondence should be addressed. Tel.: 1865-271860; Fax: 1865-271853; E-mail: derek.blake{at}pharm.ox.ac.uk.

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