Myospryn is a novel binding partner for dysbindin in muscle.

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.
Mesh Terms:
Amino Acid Sequence, Animals, COS Cells, Carrier Proteins, DNA, Complementary, Down-Regulation, Immunohistochemistry, Mice, Models, Genetic, Molecular Sequence Data, Muscle Proteins, Muscles, Precipitin Tests, Protein Binding, Protein Structure, Tertiary, RNA, Messenger, Sequence Homology, Amino Acid, Subcellular Fractions, Tissue Distribution, Transfection, Two-Hybrid System Techniques, Up-Regulation, beta-Galactosidase
J. Biol. Chem.
Date: Mar. 12, 2004
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