| First Author | Benson MA | Year | 2004 |
| Journal | J Biol Chem | Volume | 279 |
| Issue | 11 | Pages | 10450-8 |
| PubMed ID | 14688250 | Mgi Jnum | J:88863 |
| Mgi Id | MGI:3037366 | Doi | 10.1074/jbc.M312664200 |
| Citation | Benson MA, et al. (2004) Myospryn is a novel binding partner for dysbindin in muscle. J Biol Chem 279(11):10450-8 |
| abstractText | 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. |
