Members of the ATP-dependent family of chromatin remodeling enzymes play key roles in the regulation of transcription, development, DNA repair and cell cycle. Each of these enzymes are multi-subunit assemblies that hydrolyze thousands of molecules of ATP in order to change nucleosome positions, disrupt DNA-histone interactions and perhaps destabilize chromatin folding. Here I review recent studies that suggest these potent machines can be 'tamed' by one of several mechanisms: targeting their activity to localized regions, blocking their chromatin binding activity or inhibiting their remodeling activity.