Investigating the role of the deubiquitylating enzyme USP25 in cell cycle control

Proteins are molecular machines that function inside cells to regulate processes such as cell growth, division and death. Protein function is modified by the attachment of regulatory proteins such as ubiquitin. Ubiquitin modification is important in targeting proteins for destruction in the cell during cell division. Dysregulation of protein destruction can lead to inappropriate cell growth and cancer. Understanding normal protein function by modification enhances our understanding of biological processes, and identifies drugs with therapeutic value. This project will investigate how ubiquitin modification regulates cell growth and division by depleting the protein USP25 from the cell. USP25 controls the extent of ubiquitin modifications on proteins. We will investigate how USP25 functions in modulating ubiquitin on UbcH10, another protein that is important in controlling cell growth and division. This project will provide new insights into the fundamental role of USP25 in cell growth and division to help identify therapeutic anti-cancer drugs.

Faculty Supervisor:

Jose Teodoro

Student:

Partner:

University of Birmingham

Discipline:

Life Sciences

Sector:

Life Sciences (not health); Technology; Pharmaceuticals

University:

McGill University

Program: