Understanding how cells age through the lens of protein complexes.

Much of biology asks when, where, and how much of a protein is expressed. But proteins with the same sequence and abundance can exist in very different molecular forms. They can be free or assembled into complexes, interact with different partners, bind RNA, carry different post-translational modifications, and have different lifetimes.

We think of these different assembly states as distinct functional forms of a protein. Just as different transcript or protein isoforms can perform distinct functions, the same protein can occupy different molecular states with different biological roles and regulation.

Our lab uses protein assembly states as a lens for discovering biology. Rather than asking only whether a protein changes in abundance, we ask how it moves between molecular states, and what these transitions reveal about its function, regulation, and fate. We develop and apply quantitative mass spectrometry-based proteomic approaches to study these states at scale, with a particular interest in how their regulation changes with age.