Michael James Emanuele

Area of Interest

Our lab studies how cells control the destruction of proteins, a process that is essential for healthy cell function and often misregulated in rapidly proliferating cancer cells. This process is governed by the ubiquitin system, which ensures that specific proteins are removed at the right time to maintain cellular balance and prevent disease. When this system malfunctions, it can drive cancer development.

We investigate how protein degradation is regulated across multiple cancer types, including breast, ovarian, and colorectal malignancies. Our work aims to understand how disruptions in this system contribute to tumor growth and how these processes are altered by cancer therapies. A major area of our research explores how cancer-associated kinase signaling pathways interact with the protein degradation machinery. The impact of altered protein breakdown on disease progression and treatment response remains understudied, but is likely to play an important role.

Using advanced proteomics and computational tools, we map how cancer initiation and treatment reshape the cellular protein landscape. We then use molecular, cellular, and genetic approaches to determine how these changes influence cancer behaviors. We focus on two main enzyme families: E3 ubiquitin ligases, which tag proteins for destruction, and deubiquitinases (DUBs), which remove those tags and are emerging as promising therapeutic targets. Our goal is to understand how these systems are rewired in cancer and to uncover new therapeutic vulnerabilities. We are especially interested in testing emerging cancer therapies that target these pathways to improve patient outcomes.

Find publications on PubMed

Awards and Honors

• Associate Professor with tenure, American Cancer Society Research Scholar Award
• Susan G Komen Career Catalyst Research Award
• Jimmy V Foundation-Scholar Award
• Damon Runyon Postdoctoral Fellowship Award

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