Our cells contain a small protein, called ubiquitin, which safeguards the normal functions of thousands of other proteins. Ubiquitin is attached to other proteins, in a highly coordinated manner, by enzymes called ubiquitin ligases. This process of ubiquitin attachment, called ubiquitination, is very important for cell function, as it can promote or block the functions of proteins depending on the cell's needs. Indeed, ubiquitination is required for many cellular processes including the maintenance of the integrity of our genetic material. Aberrations in ubiquitination processes cause cancer.
The goal of our research is to determine (i) how ubiquitin regulates protein function, (ii) how deregulation in these processes cause cancer and (iii) how we can identify aberrant signaling pathways to be harnessed for the design of novel therapeutic strategies.
We are currently focusing on a novel class of enzymes called deubiquitinases or DUBs for short. These enzymes perform the reverse reaction of ubiquitination, i.e., removing ubiquitin from proteins in a timely manner. Failure to do so can have devastating consequences on normal cells and can promote cancer development. For instance, we are currently investigating a DUB called BAP1, which represents a major tumor suppressor, meaning that it prevents the development of cancer.
To accomplish our studies, we plan to use molecular and cellular biology approaches in conjunction with human cells that are normal or derived from cancer patients. Our research is important because these studies are highly expected to lead to the identification of vulnerabilities of cancer cells. Acquiring this knowledge is critical and will help designing improved protocols for the treatment of cancer.