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PMID:14688250
| Citation |
Benson, MA, Tinsley, CL and Blake, DJ (2004) Myospryn is a novel binding partner for dysbindin in muscle. J. Biol. Chem. 279:10450-8 |
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| Abstract |
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. |
| Links |
PubMed Online version:10.1074/jbc.M312664200 |
| Keywords |
Amino Acid Sequence; Animals; COS Cells; Carrier Proteins/chemistry; Carrier Proteins/metabolism; Carrier Proteins/physiology; DNA, Complementary/metabolism; Down-Regulation; Immunohistochemistry; Mice; Models, Genetic; Molecular Sequence Data; Muscle Proteins/chemistry; Muscle Proteins/metabolism; Muscle Proteins/physiology; Muscles/metabolism; Precipitin Tests; Protein Binding; Protein Structure, Tertiary; RNA, Messenger/metabolism; Sequence Homology, Amino Acid; Subcellular Fractions/metabolism; Tissue Distribution; Transfection; Two-Hybrid System Techniques; Up-Regulation; beta-Galactosidase/metabolism |
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Significance
Annotations
| Gene product | Qualifier | GO ID | GO term name | Evidence Code | with/from | Aspect | Notes | Status |
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