Beyond channel assembly, the CLZ coiled-coil domain may also serve as a scaffold for interactions with other proteins. Previously, it has been shown that the calmodulin binding site in the aminoterminal region of CNGB1 directly interacts with the CLZ domain of CNGA1 (refs 36,37) . Furthermore, Ca 2 + -calmodulin disrupts this interaction resulting in separation of the amino-terminal region of CNGB1 from the carboxy-terminal region of CNGA1 (ref. 38) . Also, the CLZ coiled-coil domain may be an important site of interaction for protein complexes that regulate channel activity, as has been proposed for Kv7 channels [39] [40] [41] .