Dr. Cecilia Lopez (she, her, hers)

Dr. Zurita Lopez's laboratory investigates protein arginine methyltransferases (PRMTs), enzymes that post-translationally modify (PTM) proteins by adding a methyl group to arginine residues. In particular, she focuses on PRMTs that share motifs with kinases so that she can identify substrates that are involved in PTM crosstalk. For example, PRMT7 shares a preference for an RXR motif with the kinase Akt whose binding motif is RXRXXS/T. Tentative substrates include histone proteins and PGC-1alpha. Identifying proteins and the sites at which protein arginine methylation affects phosphorylation will contribute to a greater understanding of cellular signaling.

Dr. Zurita Lopez first became introduced to post-translational modifications as a graduate student under the direction of Dr. Steven Clarke at UCLA where she studied protein arginine methyltransferases (both in humans and in lower organisms), by characterizing their modifications on various protein substrates, including uncovering methylation marks on histone proteins. She also added to the understanding of the mechanisms by which PRMTs affect cellular function. For example, she identified Ash2L as a substrate of PRMT1, a protein critically linked to proper embryonic development. As a postdoctoral researcher at Caltech, she broadened her training in biochemistry and molecular biology while studying the role of the signal recognition particle (SRP), a “zip code” that leads proteins to their proper cellular localization. At USC, under the direction of Andrea Armani, she was part of an engineering group (chemical engineering and materials science) whose focus is the characterization and development of a new photonic device, also known as a microresonator. Dr. Zurita Lopez participated in the study of these microresonators by applying them as biosensors for the study of methylation on both peptides and proteins, and for their use as detectors for early changes in cancer cells.