of protein α- and β-Dystrobrevin proteins structure consisted of four major domains, a ZZ -type zinc finger domain, two EF-hand regions, an α-helical coiled-coil domain containing a dystrophin binding site, and a tyrosine kinase substrate domain. α-Dystrobrevin 1, α-Dystrobrevin 2, and α-dystrobrevin 3 binds to the dystrophin-glycoprotein complex via the amino-terminus region. α-Dystrobrevin 1 and α-Dystrobrevin 2 bind dystrophin through a highly conserved coiled-coil domain. β-dystrobrevin is detected as a 61-kDa protein in the brain, kidney, liver, and lung. β-dystrobrevin can be distinguished from α-dystrobrevin 2 because it has lower relative mobility. Slight differences in the size of the β-dystrobrevin were observed in the brain compared with the kidney, liver, and lung. Localization α-Dystrobrevin 1 is localized in the sarcolemma and is abundant at the neuromuscular junction, and concentrated in the crest of the junctional folds. α-Dystrobrevin 2 is localized around the entire circumference of the sarcolemmal plasma membrane including the neuromuscular junction. α-Dystrobrevin 2 primarily co-localizes with dystrophin at the neuromuscular junction, while α-Dystrobrevin 1 co-localizes with both dystrophin and utrophin. α-Dystrobrevin 3 has been thought to be located on the cytoplasmic site. 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. Function 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