The location and expression pattern of β-dystrobrevin was observed by using Northern blots of mouse RNAs. A single 2.5-kb transcript was detected predominantly in the brain and kidney and to a lesser extent in liver and lung. No β-dystrobrevin transcripts were detected in skeletal and cardiac muscle even after long exposures. This evidence suggested that the β-dystrobrevin transcript was weakly expressed or absent in muscle. The fundamental role of the dystrobrevin protein family remains unclear. Much of what we do know has been observation from biochemical studies of associated proteins and the phenotypic consequences of their loss.  α-Dystrobrevin proteins are suggested to involve in the structural integrity of muscle cells by interacting with cytoskeletal binding proteins and signal transduction by interacting with syntrophin. Firstly, α-Dystrobrevin is a component of the dystrophin-glycoprotein complex, which is extremely useful for maintenance of the skeletal cell integrity. α-dystrobrevin associated with dystrophin at its coil-coil region and with a sarcoglycan-protein complex at the amino-terminal. It has been proposed to function as a structural scaffold linking the dystrophin-glycoprotein complex to the intracellular cytoskeleton. Based on the yeast two-hybrid system and co-immunoprecipitation analysis, three other proteins were identified as additional to α-dystrobrevin-binding proteins: β-synemin, syncoilin, and dysbindin. Syncoilin and β-synemin are both intermediate filament proteins. The intermediate filaments are responsible for forming the structure of the cell cytoskeleton and providing mechanical stability to the cells. Syncoilin co-localizes with α-dystrobrevin at both the neuromuscular junction and sarcolemma while β-Synemin co-localizes with α-dystrobrevin only at the neuromuscular junction. The interaction of α-dystrobrevin and β-synemin provides an additional connection between the intermediate filament system and the dytsrophin-glycoprotein complex. Dysbindin is located at the sarcolemma, and its expression in skeletal muscle is relatively low. Secondly, α-Dystrobrevins participate in intracellular signaling since they bind directly with syntrophin, which is a modular adaptor protein thought to be involved in signal transduction.