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Andrew Kusmierczyk, Assistant Professor

Current Research

Much of the work inside cells is carried out by large macromolecular protein complexes. Though biological research continues to provide important insight into the structure and function of these complexes, a considerable gap exists in understanding how these complexes are assembled in the first place. Closing this knowledge gap is key because protein complex assembly provides an important, if underappreciated, means by which cells can regulate function.

Moreover, targeting protein complex assembly could provide a novel means of pharmacologically targeting protein complex function, thereby opening up new avenues for drug design. The proteasome is a large intracellular machine responsible for the ultimate degradation of the majority of intracellular proteins. Proteasomal degradation impacts virtually every cellular process, from the cell cycle, to differentiation, to apoptosis. Moreover, targeted destruction removes damaged or misfolded proteins, which may otherwise interfere with normal cellular function.

Research in my laboratory aims to understand how the proteasome itself is assembled. We are interested in determining how the regulation of proteasome assembly can be a means to regulate not just proteasome function itself, but also the myriad of other processes that the proteasome is involved in.

My laboratory is also interested in designing novel experimental systems to study proteasome assembly in vivo and in vitro, with a long-term goal of developing assays that will enable us to screen for proteasome assembly inhibitors. We use biochemical, molecular and cell biological, as well as genetic techniques to address our experimental questions, using the yeast Saccharomyces cerevisiae as a model organism. Ultimately, the lessons learned from studying proteasome assembly can shed light on the assembly of other multi-protein complexes as well.