Steven B. McMahon, PhD
Professor and Chair, Department of Biochemistry & Molecular Biology
Associate Provost, Thomas Jefferson University
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Steven B. McMahon, PhD
Professor and Chair, Department of Biochemistry & Molecular Biology
Associate Provost, Thomas Jefferson University
Expertise & Research Interests
Our group has a long-standing interest in understanding the biochemical events that are deregulated to cause alterations in broad transcriptional programs in human cancer. As such, our research focuses on the two most commonly mutated transcription factors, MYC and p53, that are critical to cancer progression. We are currently focused on defining precisely how MYC and p53 are regulated in cancer cells, how the transcription programs they control are altered in cancer, and ultimately what essential cellular processes are impacted by these changes. Collectively, these studies have identified previously unknown nodes in these pathways that may represent potential therapeutic targets.
Current Research Projects
- understand the role of altered mitochondrial transcription in the ability of MYC to reprogram cellular metabolism during malignant transformation.
- identify the mechanism by which post-translational modifications control the ability of the p53 tumor suppressor to selectively activate distinct transcriptomes.
- define the contribution of genetic lesions in subunits of the human SAGA coactivator complex to human cancer.
Education
PhD, Immunology, University of Pennsylvania
MS, Physiology, Temple University
BS, Biology, Albright College
Publications
- Non-redundant roles for the human mRNA decapping cofactor paralogs DCP1a and DCP1b
- ARID1A-BAF coordinates ZIC2 genomic occupancy for epithelial-to-mesenchymal transition in cranial neural crest specification
- A β-Catenin-TCF-Sensitive Locus Control Region Mediates GUCY2C Ligand Loss in Colorectal Cancer
- Distinct mechanisms control genome recognition by p53 at its target genes linked to different cell fates
- The SAGA complex regulates early steps in transcription via its deubiquitylase module subunit USP22