Regulating Protein Stability in Mammalian Cells Using Small Molecules, by Thomas Wandless and colleagues is featured in this month’s issue of Cold Spring Harbor Protocols. This technique provides a rapid, reversible, and tunable method for studying the activity of a protein of interest in cells. The protein is attached to a destabilization domain, and the resulting fusion proteins are unstable and degraded, except in the presence of small ligands. The speed of small-molecule binding makes it an attractive alternative to studying gene function using RNA interference (RNAi). Wandless’ group also provides a second protocol, A General Method for Conditional Regulation of Protein Stability in Living Animals.

Like all of our featured articles, Regulating Protein Stability in Mammalian Cells Using Small Molecules is freely available to subscribers and non-subscribers alike.