BYU

Abstract by Collin Nelson

Personal Infomation


Presenter's Name

Collin Nelson

Degree Level

Undergraduate

Abstract Infomation


Department

Chemistry and Biochemistry

Faculty Advisor

Barry Willardson

Title

Inhibition of Molecular Chaperones in Cancer Cells

Abstract

Molecular chaperones are a class of proteins that prevent protein aggregation and ensure nascent proteins are folded into their correct 3-dimensional shape.  Chaperones play an important role in many signaling pathways in cell.  We have previously shown that the chaperonin CCT folds proteins in two essential signaling systems: G protein complexes G-beta/gamma which act as important switches for turning many cell signals on and off and the MTORC1 pathway which is critical for cell growth and survival.  In many cancer cells these signals are overexpressed.  Previous research has suggested that the peptide CT20P inhibits CCT function.  We show that CT20P inhibits CCT mediated assembly of both G-beta/gamma and the MTORC1 pathway.  Additionally, we have shown specific binding of CT20P to CCT.  These results suggest that CT20P inhibits CCT function and can help to mitigate the overexpression of cell signaling found in cancerous cells.