Phenotypic Characterization of Allelic Variation within the HEAT Repeats of the Mechanistic Target of Rapamycin (mTOR)
Location
Old Dominion University, Learning Commons at Perry Library, West Foyer
Start Date
4-8-2017 8:30 AM
End Date
4-8-2017 10:00 AM
Description
The mammalian target of rapamycin (mTOR) is a kinase responsible for cell growth and metabolism and has been linked to tumor growth. An allelic variant (R628C) found in the HEAT repeats of mTOR, found in Balb/c mice, contributes to tumor susceptibility. HEAT repeats are known to be sites of protein-protein interactions, dimerization, and allow for proper localization. The goal of this study is to further elucidate the functional significance of HEAT repeats in TOR biology and show how allelic variation in the HEAT repeats may contribute to tumor susceptibility. Our results have shown differential binding of mTORC1/2 partners to mTOR in cells expressing the allelic variant. Studies are ongoing to assess binding to other mTORC1/2 complex partners, dimerization, and localization of the allelic variant. Our findings will model activation of mTOR signaling.
Presentation Type
Poster
Phenotypic Characterization of Allelic Variation within the HEAT Repeats of the Mechanistic Target of Rapamycin (mTOR)
Old Dominion University, Learning Commons at Perry Library, West Foyer
The mammalian target of rapamycin (mTOR) is a kinase responsible for cell growth and metabolism and has been linked to tumor growth. An allelic variant (R628C) found in the HEAT repeats of mTOR, found in Balb/c mice, contributes to tumor susceptibility. HEAT repeats are known to be sites of protein-protein interactions, dimerization, and allow for proper localization. The goal of this study is to further elucidate the functional significance of HEAT repeats in TOR biology and show how allelic variation in the HEAT repeats may contribute to tumor susceptibility. Our results have shown differential binding of mTORC1/2 partners to mTOR in cells expressing the allelic variant. Studies are ongoing to assess binding to other mTORC1/2 complex partners, dimerization, and localization of the allelic variant. Our findings will model activation of mTOR signaling.