https://orantinibinhibitor.com..../recognition-associa
Here, using man cellular outlines, fluorescence microscopy, and pulldown and immunoblotting assays, we reveal that α-dystrobrevin (α-dbn), an intracellular element of the dystrophin glycoprotein complex, directly and robustly promotes the stability of αkap in a concentration-dependent manner. Mechanistically, we found that the phosphorylatable tyrosine residues of α-dbn are essential for the security of α-dbn it self as well as its connection with αkap, with replacement of three tyrosin
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