News
News
Congratulations, Dr. McKayla Ford!
Monday, May 18, 2026
On May 18, 2026 BGG student McKayla Ford successfully defended her doctoral thesis. McKayla Joined BGG PhD program in 2020 and Dr. Paula Vertino's lab in the fall of 2021. Her research has involved dissection of the relationship between DNA sequence, DNA structure and transcriptional dynamics.
Abstract:
To control gene expression and allow for differentiation, regulation of the transcriptional process is vital. CpG islands (CGI), regulatory regions within DNA with a specific sequence and chromatin signature, support transcription by acting as promoters and enhancers. In this dissertation, the role of CpG islands in the regulation of transcription is examined, with a specific focus on the impact of the transition from CGI to non-CGI DNA has on early elongation. Sequence and structural characteristics of the CGI are also studied throughout this work in relation to their connection to transcription
Isaac Harris, Ph.D. publishes paper on 'Catabolism of extracellular glutathione supplies cysteine to support tumours' in Nature
Friday, March 27, 2026
Recently, BGG Program Director, Isaac Harris published a paper in Nature on “Catabolism of extracellular glutathione supplies cysteine to support tumours”.
Abstract:
Restricting amino acids from tumours is an emerging therapeutic strategy with substantial promise1. Although typically considered an intracellular antioxidant with tumour-promoting capabilities2, glutathione (GSH), as a tripeptide of cysteine, glutamate and glycine, can be catabolized to release amino acids. The extent to which GSH-derived amino acids are essential to cancers is unclear. Here we show that depletion of intracellular GSH does not alter tumour growth and extracellular GSH is highly abundant in the tumour microenvironment, highlighting the potential importance of GSH outside tumours. Supplementation with GSH rescues cancer cell survival and growth in cystine-deficient conditions, and this rescue depends on the catabolic activity of γ-glutamyltransferases. Finally, pharmacological targeting of the activity of γ-glutamyltransferases prevents the breakdown of circulating GSH, reduces tumour cysteine levels and slows tumour growth. Our findings indicate a non-canonical role for GSH in supporting tumours by acting as a reservoir of amino acids. Depriving tumours of extracellular GSH or inhibiting its breakdown is potentially a therapeutically tractable approach for patients with cancer. Furthermore, these findings change our view of GSH and how amino acids, including cysteine, are supplied to cells.