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Journal of Undergraduate Research

Keywords

bone morphogenetic protein 2, Bmp2, inositol, triphosphate receptor 1

College

Life Sciences

Department

Microbiology and Molecular Biology

Abstract

Bone morphogenetic protein 2 (Bmp2) is a well-characterized secreted transforming growth factor. Researchers in the lab of Dr. Laura Bridgewater, Brigham Young University, discovered a novel nuclear variant of Bmp2 (nBmp2)1. Preliminary data indicates that mice not expressing nBmp2 have difficulty regulating intracellular Ca2+ (unpublished). Seeking to find a molecular explanation for this observation, I performed a yeast two-hybrid (Y2H) screen to identify putative binding-partners of nBmp2. My results indicate nBmp2 binds Phospholipid scramblase 1 (PLSCR1). Zhou et al2 have shown that PLSCR1 directly binds a 15 DNA base pair sequence (hereafter called P1) ~100 base pairs upstream of the Inositol 1,4,5-triphosphate receptor 1 (Itpr1) gene. This sequence was found in the promoter (DNA that regulates the expression of a gene) for Itpr1. The interaction between Plscr1 and P1 increases the expression of Itpr1 protein in mice. Itpr1 is an additional important regulator of intracellular Ca2+ levels. I hypothesized that one significant way nBmp2 affects Ca2+ regulation is by controlling the transcription of Itpr1 through manipulating the interaction between Plscr1 and P1. I sought to test this possibility by constructing a transcriptional activation reporter assay.

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