The analysis of consequences resulting after experimental elimination of gene 
function has been and will continue to be an extremely successful strategy in 
biological research. Mutational elimination of gene function has been widely 
used in the fly Drosophila melanogaster. RNA interference is used extensively as 
well. In the fly, exceptionally precise temporal and spatial control over 
elimination of gene function can be achieved in combination with sophisticated 
transgenic approaches and clonal analyses. However, the methods that act at the 
gene and transcript level cannot eliminate protein products which are already 
present at the time when mutant cells are generated or RNA interference is 
started. Targeted inducible protein degradation is therefore of considerable 
interest for controlled rapid elimination of gene function. To this end, a 
degradation system was developed in yeast exploiting TIR1, a plant F box 
protein, which can recruit proteins with an auxin-inducible degron to an E3 
ubiquitin ligase complex, but only in the presence of the phytohormone auxin. 
Here we demonstrate that the auxin-inducible degradation system functions 
efficiently also in Drosophila melanogaster. Neither auxin nor TIR1 expression 
have obvious toxic effects in this organism, and in combination they result in 
rapid degradation of a target protein fused to the auxin-inducible degron.