Digitized Honors Theses (2002-2017)

Date of Award

5-2012

Document Type

Undergraduate Thesis

Degree Name

BS

Department

Biomedical Sciences

Faculty Mentor

Rajeev Samant

Abstract

Breast cancer is a worldwide health issue, affecting millions of people and accounting for a large proportion of cancer deaths. The invasiveness of breast cancer is modulated by a number of proteins. One such protein, MRJ, has been observed to decrease the metastatic potential of breast cancer cells when it localizes to the nucleus. The mechanisms by which the small isoform of MRJ, MRJ(S), localizes to the nucleus have not been clearly identified. It is possible that a domain of MRJ(S) interacts with a protein or protein complex which shuttles it to the nucleus. Elucidation of this mechanism would allow for more extensive study of MRJ's possible therapeutic benefits in cancer. Thus, our lab designed a number of experiments to more definitively identify which domain of MRJ(S) and which other proteins are responsible for its nuclear import. A number of eGFP-tagged mutation and deletion constructs were expressed in cancer cells and subject to fluorescence microscopy to identify their subcellular localization. This indicated a 22 amino acid stretch at the C-terminus as a possible stress sensing region. In addition, potential interactors were co-immunoprecipitated with MRJ(S) and their identities conjectured based on their apparent size on a silver stained SDS-PAGE gel, the most notable of which were BRMSl, HDAC4, and NFATc3. We were able to both narrow down the domain of MRJ(S) which is likely involved in nuclear import and to identify a few known interactors of MRJ(S) which may be instrumental in its nuclear import.

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