Emily graduated from Swarthmore College in 2009 with a major in Chemistry and a minor in Religion. While at Swarthmore, she worked in Kathleen Siwicki’s lab to develop techniques to visualize the expression pattern of b-octopamine receptors in the Drosophila melanogaster brain. Later she joined the lab of Kathleen Howard, using electron paramagnetic resonance spectroscopy to measure the conformational changes of the M2 proton channel in lipid bilayers. After graduation, Emily spent a year as a research assistant in Vlad Denic’s lab at Harvard University. In the Denic lab she helped define the mechanism by which tail-anchored proteins are post-translationally inserted into the ER membrane.
Wanting to continue in the field of membrane protein biochemistry, Emily is working in the MacKinnon lab to understand the regulation of inwardly rectifying potassium (Kir) channels. It has been reported in cell-based studies that channels in every Kir subfamily require interaction with the charged lipid PIP2 for activation. However, Emily has shown in a fully reconstituted flux assay that while Kir2.1 and Kir2.2 channels appear to have a strict PIP2 requirement, Kir1.1 (also known as ROMK) channels have significant activity in the absence of PIP2. In order to better understand the mechanism by which this lipid activates Kir channels, Emily is monitoring the activity of single Kir channels reconstituted in a horizontal bilayer setup. She will use this mechanistic insight to evaluate models of PIP2 activation suggested by structural data from the lab. Since many Kir channels lack specific inhibitors, preventing a thorough exploration of their activity in vivo, Emily plans to identify small molecules that block ROMK to better understand its function in native tissues.
Representative recordings of single cKir2.2 channels reconstituted in DPhPC:POPA (3:1) bilayers in the absence and presence of PIP2.