HAMP domains communicate between input and output signalling elements in bacterial proteins. In the Tsr chemoreceptor, they convert axial movement of transmembrane helix 2 into changes in packing of the cytoplasmic kinase-control module (KCM). Zhou et al. suggest transmembrane helix 2 'tugs' on HAMP to destabilize x-da packing of the parallel four-helix bundle of the HAMP homodimer. Attractants would inhibit tugging. HAMP stability may be inversely related to stability of the a-d packing of the anti-parallel four-helix bundle of KCM, a relationship possibly facilitated by HAMP/KCM helical mismatch. The beauty of this idea lies in its simplicity and testability.