February 6, 2019
University of Pittsburgh professor to present Biochemistry and Molecular Biophysics Seminar today
Submitted by Biochemistry and Molecular Biophysics
Allyson O'Donnell, assistant professor of biological sciences at the University of Pittsburgh, will be the featured speaker for the College of Arts and Sciences' Biochemistry and Molecular Biophysics Seminar at 4 p.m. Feb. 6 in 120 Ackert Hall. She will present "Ticket to Ride: Alpha-arrestin regulation of selective protein trafficking."
O'Donnell earned her doctorate in biochemistry and molecular biology from Dalhousie University in 2004 under Richard Singer and Gerald Johnston. She began researching alpha-arrestin regulation of protein trafficking as a postdoctal fellow at Stanford University with Martha Cyert, followed by work at the University of California, Berkeley with Jeremy Thorner. In 2012, she began work with Alexander Sorkin as a research assistant professor in cell biology at the University of Pittsburgh. O'Donnell then had the opportunity to set up her own independent research lab in biological sciences at Duquesne University in 2015. In 2016, she received a National Science Foundation Career grant for "Regulation of cargo selection and ubiquitination by protein trafficking adaptors." She then returned to the University of Pittsburgh in August 2018 as assistant professor of biological sciences.
Presentation abstract: Cells rapidly reshuffle proteins at the cell surface in response to environmental change, aging and/or protein misfolding; new proteins are sent to the cell surface while those that are no longer functional are selectively removed. How does the cell make the "decision" to change a specific protein's localization? Knowledge of the factors that drive this cellular decision is critical to human health; nearly 50 percent of drugs target receptors at the cell surface, highlighting the importance of understanding how membrane protein localization is controlled. The β-arrestins, a well characterized family of trafficking adaptors, control the localization of G-protein coupled receptors (GPCRs) and are themselves therapeutic targets. However, β-arrestins are only a small, recently evolved branch of the much larger arrestin family. The more ancestral α-arrestins, widely conserved but poorly characterized proteins, are the primary focus of my research. Using Saccharomyces cerevisiae as a model, O'Donnell has shown that α-arrestins regulate GPCR signaling and operate in previously unexpected trafficking pathways, including clathrin independent endocytosis and in intracellular sorting. In addition, O'Donnell has identified α-arrestin interactions with signaling regulators, membrane proteins and vesicle coat proteins, and have begun to define the molecular mechanisms underlying α-arrestin-mediated trafficking. All of the α-arrestin-interacting partners O'Donnell has identified are conserved from yeast to man; mechanisms of α-arrestin function defined by my work in yeast are proving to be conserved for the mammalian α-arrestins. We are now at the point of transitioning into a mammalian cell system, using our results in yeast to guide targeted studies. Research in O'Donnell's lab employs biochemical, molecular, genetic and advanced cell biology methods to study how α-arrestins regulate membrane protein localization. Our work contributes to emerging paradigms of membrane trafficking and post-ER quality control, and has therapeutic and disease implications.