High impact information on UTRN

• These data suggest that utrophin could replace dystrophin functionally in dystrophic muscle [1].
• Here we demonstrate that expressed regions of the predicted actin binding domain in the NH2 terminus of utrophin are able to bind to F-actin in vitro, but do not interact with G-actin [1].
• Like dystrophin, utrophin has been shown to be associated with a membrane-bound glycoprotein complex [1].
• The utrophin actin binding domain was also able to associate with actin-containing structures, stress fibres and focal contacts, when microinjected into chick embryo fibroblasts [1].
• Moreover, this utrophin domain binds to non-muscle actin with a approximately 4-fold higher affinity than to skeletal muscle actin [1].

Other interactions of UTRN

• Moreover, the predicted structure of the calponin CH domain is identical to that found by X-ray studies of the spectrin, fimbrin and utrophin CH domains [2].

References