The cytoskeletal protein obscurin has previously been studied only in muscular cells, where it was first characterized. It is known that obscurin plays a role in cell mobility, and if not functioning correctly, can lead to cancer as a result of unregulated movement. Literature has shown that this protein is most often mutated in breast and colorectal cancers. In novel experiments, obscurin is added to cell cultures via adenovirus infection as opposed to previous methods utilizing knockout techniques. The effects of this addition have been measured in colocalization studies, timelapse velocity analysis, and lipid assays. Each of these experiments has shown that there are multiple domains within the obscurin construct that oversee cellular motility regulation, namely, the Rho-GEF and PH domains, as well as certain segments of the unstructured region near the C terminus of the protein.
Peter J. Henry (Sun,) studied this question.