J. Wylie Nichols, PhD

Professor Emeritus

Emory University School of Medicine

Office: 600 Whitehead Building

Email: wylie.nichols@emory.edu

Additional Contact Information

Mailing Address:

Department of Physiology

615 Michael Street

Atlanta, GA 30322


Education: Ph.D., University of California, Davis, 1979


The goal of my research is to better understand how the lipid components of cellular membranes are organized, how this organization is related to cellular function, and how these cellular functions are regulated by dynamic reorganization of the membranes. One particular area of focus is to understand how the distribution of aminophospholipids across the plasma membrane is established and regulated. The importance of this problem is reflected by the fact that essentially all eukarytotic cells maintain a non-random distribution of phospholipids across their plasma membranes. The reason for this universal property of cells is to sequester phospholipids with chemically reactive head groups to the cytosolic leaflet, where they participate in protein recognition and cell signaling, and to expose phospholipids with un-reactive head groups to the outer leaflet, where they produce an inert surface that is less likely to be damaged by external chemicals and toxins. This asymmetric distribution of phospholipids is maintained in a steady-state by the activity of flippases and floppases that actively transport phospholipids across the plasma membrane. Our goal is to identify the flippases and floppases that establish the asymmetry and to determine how their activity is regulated by intracellular signals. To address these problems, we pioneered the use of fluorescent-tagged phospholipids to visualize and assay phospholipid transport in the budding yeast, Saccharomyces cerevisiae. This approach has allowed us to combine genetic, biochemical, and molecular biological techniques, leading to the identification of several phospholipid flippases and floppases in yeast which are highly conserved in higher eukaryotes. In addition to identifying additional flippases and floppases, we are interested in understanding the signaling mechanisms that regulate the activity of these transporters.