Nutrients in. Waste out. Everyone and almost every living thing does it, even at the cellular level. It seems like a simple enough concept: to survive, cells have to have a way to move different types of molecules in and out of themselves. It’s how they take in food, get rid of waste, send signals to each other, sense their environment, and more. But the reality is much more complex. Transmembrane proteins — those embedded in the cell membrane and of which some are responsible for this transmission of molecules — are notoriously hard to study and understand.
University of Wisconsin–Madison associate professor of biochemistry Katherine Henzler-Wildman has dedicated her lab to doing a deep dive into these transporters and channels. In particular, part of the lab has been focusing on one called EmrE, which is present in the bacteria E. coli. It’s part of a family of bacterial transporters called multidrug resistance transporters because most confer resistance to antibiotics. Through a series of studies that exemplify the incremental process of basic scientific discovery, her lab is uncovering how exactly this transporter works — and the secret could lie in its tiny molecular “tail.”
“I’m fascinated by membrane proteins, channels and transporters in particular, because that’s how molecules move in and out across the membrane barrier and that’s a super important process,” Henzler-Wildman says. “These relatively big conformational changes are regulated by protons, something so small. These transporters can be a bit of a black box so it’s important to understand how they work.”
Read more about this research from the Henzler-Wildman Lab at the link below.