Christine Mayr, MD, PhD is a Member of the Cancer Biology and Genetics Program at Memorial Sloan Kettering Cancer Center in New York. Her research studies how 3′ untranslated regions (3′UTRs) regulate protein functions and how mRNAs contribute to cytoplasmic organization. Her work takes a multidisciplinary approach to study how RNA regulates protein activity.

Dr. Christine Mayr exemplifies the core values of The Pershing Square Foundation, which bets on bold, early-career scientists and encourages them to take risks at a moment when traditional funding is lacking.

 Dr. Mayr was awarded the Pershing Square Sohn Cancer Prize in 2015. The following year, she won the highly prestigious NIH Director’s Pioneer Award and had an influx of capital to her lab.

 PSF’s investment in Dr. Mayr led to her exciting discovery of a new membranelles organelle, called the TIS granule in 2018 (Ma & Mayr, 2018). TIS granules are formed by the RNA-binding protein TIS11B together with its bound mRNAs. TIS granules form a mesh-like compartment with a biophysically and biochemically distinct environment compared to the surrounding cytosol. This mRNA-based subcellular compartment enables formation of specific and functionally relevant protein complexes that cannot be established outside this environment. This previously unidentified cellular structure added to the field’s collective understanding of the intricate processes involved in gene expression and protein synthesis within cells, which will have potential implications on cancer, neurological disorders, and other diseases.

 PSF’s partnership with Dr. Mayr has since expanded far beyond her original prize in 2015. In 2020, she received one of 19 grants the Foundation rapidly deployed to support novel COVID-19 research. More recently, inspired by her revolutionary findings of the TIS granule, the Foundation continues to fund the Mayr lab. After her award term had concluded, Dr. Mayr was asked to join the Pershing Square Sohn Cancer Research Alliance’s Scientific Review Council to lend her expertise to assist the foundation in selecting top applicants to receive Prize in years to come.

Dr. Mayr has significantly advanced our understanding of the molecular basis of cancer and RNA biology, with implications for a wide array of other diseases. Her discoveries, which were in part funded by PSF, include research papers in Nature, Cell, and Molecular Cell, and were also featured on the cover of MSK news. Her lab is already building on her PSF-funded discoveries. First, the Mayr lab found that it makes a big difference where in a cell’s cytoplasm mRNAs get translated into proteins, which could have implications for increasing or altering the production of proteins in mRNA vaccines and therapies. Second, Dr. Mayr and her team have uncovered another new structure inside of cells. This assembly, dubbed the FXR1 network, is substantially larger, extending to cover the whole cytoplasm, and acts as a novel type of scaffold for signaling pathways. The signaling pathways that take advantage of the network are important for changes in cell shape, for adhesion and migration, and for the transmission of force, and might also play a key role in brain function. It is our sincere hope that Dr. Mayr’s support from PSF paired with her NIH award has allowed her the freedom to pursue her research persistently.  PSF is grateful to have Dr. Mayr in our community of brilliant scientists and will be by her side for years to come.

• Chen, X., Fansler, M.M., Janjoš, U., Ule, J., and Mayr, C. (2024). The FXR1 network acts as signaling scaffold for actomyosin remodeling. Cell, in press. Also on bioRxiv, 2023.2011.2005.565677.

• Fansler, M.M., Mitschka, S., and Mayr, C. (2024). Quantifying 3′UTR length from scRNA-seq data reveals changes independent of gene expression. Nature communications 15, 4050. Link to publication: https://www.nature.com/articles/s41467-024-48254-9

• Luo, Y., Pratihar, S., Horste, E.H., Mitschka, S., Mey, A.S.J.S., Al-Hashimi, H.M., and Mayr, C. (2023). mRNA interactions with disordered regions control protein activity. bioRxiv, 2023.2002.2018.529068.

• Horste, E.L., Fansler, M.M., Cai, T., Chen, X., Mitschka, S., Zhen, G., Lee, F.C.Y., Ule, J., and Mayr, C. (2023). Subcytoplasmic location of translation controls protein output. Mol Cell 83, 4509-4523.e4511.

• Mitschka, S., Mayr, C. (2022) Context- specific regulation and function of mRNA alternative Polyadenylation. Nature reviews Molecular Cell Biology, 12: 779-796

• Kwon, B., Fansler, M.M., Patel, N.D., Lee, J., Ma, W., and Mayr, C. (2022). Enhancers regulate 3’ end processing activity to control expression of alternative 3’UTR isoforms. Nature communications 13, 2709

• Chen, X., and Mayr, C. (2022). A working model for condensate RNA-binding proteins as matchmakers for protein complex assembly. Rna 28, 76-87.

• Lee, S. H., & Mayr, C. (2019). Gain of Additional BIRC3 Protein Functions through 3'-UTR-Mediated Protein Complex Formation. Molecular cell, 74(4), 701–712.e9. https://doi.org/10.1016/j.molcel.2019.03.006

• Ma, W., & Mayr, C. (2018). A Membraneless Organelle Associated with the Endoplasmic Reticulum Enables 3'UTR-Mediated Protein-Protein Interactions. Cell, 175(6), 1492–1506.e19. https://doi.org/10.1016/j.cell.2018.10.007

• Mayr C. (2017). Regulation by 3'-Untranslated Regions. Annual review of genetics, 51, 171–194. https://doi.org/10.1146/annurev-genet-120116-024704