Understanding the Chaperone Code in cancer

Hsp70 is a well-conserved molecular chaperone that binds and folds a a large proportion of proteins in the cell. Many cancer proteins are inherently unstable and need chaperones to maintain activity. We are interested in creating novel anticancer therapies based on fine-tuning chaperone function rather than completely abolishing it.

Although Hsp70 has been studied for decades, there is still little known about the effect of the large number of post-translational modifications (chaperone code) on Hsp70 function at the cellular and organismal level. We are interested in understanding the cellular conditions, and enzymes that add and remove these modifications as well as the effect these PTMs on global chaperone interactions.

Yeast expressing Ssa1-GFP

Prostate cancer spheroids treated with the chaperone inhibitor 116-9e. 

We use a range of cells and tissues for our work, but primarily we use the model organism budding yeast (saccharomyces cerevisiae) and follow up with analyses in tissue culture and 3D organoids.

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Tribrid Fusion Mass Spectrometer

CRISPR-editing Hsc70 to add an epitope tag at the genomic level


We utilize a range of molecular and cellular technologies to understand the complex regulation of chaperones in yeast and mammalian cells, including high-resolution microscopy, mass spectrometry, CRISPR-mediated genome engineering, protein purification and mutagenesis, as well as high-throughput chemogenomic screens.

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We are excited to be a part of the UNC Charlotte Genome Integrity Group. For more info, please see here!

Keywords: protein-protein interactions, protein folding, CRISPR-CAS9, breast cancer, signal transduction, phosphorylation, Hsp70.

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