Investigating the Association between Emerin and Btf

Abstract

<p>Btf is a nuclear speckle protein that can operate as a transcriptional repressor, and that when over expressed in a cell, causes apoptosis. Apoptosis is a genetically controlled process of cell suicide that plays a critical role in maintaining homeostasis and preventing disease. Emerin is an integral membrane protein of the inner nuclear membrane in vertebrates, and it is predominantly located at the inner nuclear membrane. It is also a nuclear-lamina associated protein. A yeast two-hybrid screen determined that Btf binds with emerin. A mutation in the gene encoding emerin, EMD, is responsible for the disease Emery-Dreifuss Muscular Dystrophy (EDMD). A specific mutation (S54F) in the Btf-binding region of emerin is found in some EDMD patients and may disrupt emerin binding to Btf. Emery-Dreifuss Muscular Dystrophy is one of the nine types of muscular dystrophy, a group of degenerative genetic diseases that predominantly affect voluntary muscles. Its onset is generally around ten years of age, with symptoms of weakness and wasting of the shoulder, upper arm, and calf muscles, as well as joint stiffening. The disease typically progresses slowly and cardiac complications are common. Interestingly, results from our lab show that Btf is upregulated during muscle cell differentiation, which may increase the extent to which Btf can bind with emerin. In order to fully understand the mechanism for disease in patients with various emerin mutations, it is important to understand how emerin interacts with other cellular proteins. My project aims to understand the association of emerin and Btf in muscle cells and other cell types. If we can tie disruption of Btf-emerin interaction to EDMD mutations, the ultimate goal of this research will be to develop therapeutic treatments to repair Btf-emerin association in patients with EDMD.</p><p>This presentation occurred at the Wright State University Campus-Wide Celebration of Research, Scholarship and Creative Activities on April 8, 2011</p>