BPS2026 - Cryo-EM techniques aimed at the tropomyosin junction

Actin is a ubiquitous protein that organizes into filamentous networks of vastly different morphologies in order to accommodate functions, such as cell migration, cytokinesis, and mechanosensing within eukaryotic cells. Tropomyosins constitute a large, conserved family of actin-binding proteins that regulate most if not all of these actin network-mediated processes. In mammalian cells, four tropomyosin genes code for upward of 40 isoforms through differential splicing. Although it is thought that the functions of different tropomyosin isoforms are non-redundant from one-another, their chemical and distribution similarities make it difficult to study their sequence to function relationship within the context of the cell. The Mullins Lab has characterized Drosophila Schneider 2 cells as expressing only three isoforms of tropomyosin, making them a useful model system for studying tropomyosin functions. More recent work elucidated novel behaviors of these tropomyosins in their structures. Here, I present work on using cryo-electron microscopy in order to understand the structural idiosyncracies of Drosophila tropomyosin.