Shedding New “Light”—Fluorescent proteins (FPs) have long been vital tools for tracking proteins within live cells. When fused to a protein of interest, FPs can “report” the location and levels of that specific protein. But popular FPs can be unreliable, especially when fused to proteins made within a cell’s endoplasmic reticulum (ER). Properties of the FPs can be susceptible to inactivating reactions with the cellular environment, making the proteins dark and leading to inaccurate “reporting.” In the July 9, 2015 issue of Nature Communications, Dr. Erik Snapp and colleagues describe a new set of FPs that can be used in diverse cellular environments including the ER, mitochondria, and bacteria, to faithfully report the location and levels of fusion proteins. These new FPs, called moxFPs, could become essential tools for studying protein function within many different cellular compartments. Dr. Snapp is associate professor of anatomy & structural biology. The lead author on the paper was Lindsey Costantini, a recent graduate from Dr. Snapp’s team.
Posted on: Thursday, August 20, 2015