Courtney is originally from a very small town named South Boston…in Virginia (no, not Massachusetts--a common misunderstanding). As an undergraduate at the University of Virginia, she began her research career studying a post-translational modification of the microtubule cytoskeleton in P. Todd Stukenberg’s lab. Her scientific interests have since gravitated towards questions concerning the cytoskeleton and its binding partners.
Following her time at UVA, she accepted a yearlong scholarship at the University of Cambridge in England. She learned a number of biochemical techniques in the lab of Darerca Owen and Helen Mott and studied a protein involved in the regulation of the actin cytoskeleton. After receiving a Master’s at Cambridge, she conducted her doctoral work at the University of California, San Francisco in Ron Vale’s lab. She returned to the microtubule cytoskeleton for her doctoral work and studied the microtubule-based motor complex dynein. During her PhD, she solved protein structures and used them in combination with basic evolutionary analyses to pinpoint conserved protein binding interfaces, triggering her interest in using evolutionary analyses to inform cytoskeletal function.
The cytoskeleton is generally thought to evolve under extreme selective constraint due to its essentiality in many eukaryotic functions. Although this is true for the majority of cytoskeletal proteins, a subset of such proteins evolves rapidly, indicative of an adaptive advantage for genetic innovation. Courtney joined Dr. Harmit Malik’s lab to develop a research program focused on using these previously ignored signatures of evolutionary innovation to discover new cytoskeletal genes and their functions. During her postdoc, Courtney has focused on divergent members of one particular cytoskeletal family, the actin-related protein (Arp) superfamily. Her postdoctoral work has demonstrated that Arp diversification is recurrent in several animal lineages, and consistently exhibits specialized roles in the male germline. Courtney’s future lab will combine evolution, biochemistry, cell biology, and organismal biology to decipher the causes and consequences of all diversifying cytoskeletal proteins.
Schroeder, C.M., Tomlin, S., Valenzuela, J.R., and Malik, H.S. (2020) A rapidly evolving actin mediates fertility and developmental tradeoffs in Drosophila. BioRxiv
Schroeder, C.M., Valenzuela, J.R., Mejia Natividad, I., Hocky, G.M. and Malik, H.S. (2019) A burst of genetic innovation in Drosophila actin-related proteins for testis-specific function. Molecular Biology and Evolution vol. 37, 757-772.
Clayton, N.S., Fox, M., Vicente-Garcia, J.J., Schroeder, C.M., Littlewood, T.D., Wilde, J.I., Corry, J., Krishnan, K., Zhang, Q., Wakelam, M.J.O, Brown, M.J.B., Crafter, C., Mott, H.R. and Owen, D. (2019) Assembly of novel, nuclear dimers of the PI3-Kinase regulatory subunits underpins the pro-proliferative activity of the Cdc42-Activated Tyrosine Kinase, ACK. BioRxiv DOI: 10.1101/791277.
Schroeder, C.M. and Vale, R.D. (2016) Assembly and Activation of Dynein-Dynactin by the Cargo Adaptor Protein Hook3. Journal of Cell Biology vol. 214, 309–318.
Bhabha, G.*, Johnson, G. T.*, Schroeder, C. M. and Vale, R. D. (2016). How Dynein Moves Along Microtubules. Trends Biochem. Sci. 41, 94–105. *Equal contribution
Schroeder, C. M., Ostrem, J. M. L., Hertz, N. T. and Vale, R. D. (2014). A Ras-like domain in the light intermediate chain bridges the dynein motor to a cargo-binding region. eLife 3, e03351.