In the Hunter lab, I will explore whether breast cancers show altered patterns of histidine phosphorylation. Many cancers are characterized by atypical modifications of proteins; in particular, those that regulate cell growth and proliferation, such as phosphorylation. This modification involves the addition of a phosphate group to specific amino acids, typically tyrosine, serine, and threonine. Histidine can also be a target for phosphate addition, but its study has been neglected because it is highly unstable. Recently, the Hunter lab developed molecular biology tools for studying this modification and has found that it is enriched in liver tumors. However, it is still unknown if other types of cancers show a similar pattern. I am particularly interested in breast cancer and, by applying these novel methods, I will determine whether histidine phosphorylation is altered in breast, human and mouse tumors and cell lines. Furthermore, I will assess which proteins are targeted by this modification and generate mouse models that are either missing these target proteins or overproduce them. This work could lead to the development of highly directed therapies for breast cancer—especially the aggressive triple-negative subtype, for which no targeted molecular treatments exist.