The SK channel gating mechanism is controlled by intracellular calcium levels. Calcium enters the cell via voltage activated calcium channels as well as through NMDA receptors.  Calcium does not directly bind to the SK channel. Even in the absence of calcium, the SK channel binds to the C-lobe of the protein calmodulin (CaM). When the N-lobe binds calcium, it traps the S4-S5 linker on the intracellular subunit of the SK channel. When each of the four S4-S5 linkers are bound to the N-lobe of calmodulin, the SK channel changes conformation. Calmodulin pushes the S4-S5 linker to allow the expansion of the S6 bundle crossing, leading to opening of the pore. The idea that this transitions the channel from a tetramer of monomers to a folded dimer of dimers, which results in rotation of the CaM-binding domains is now abandoned, and the most recent observations are not compatible with the proposal that this rotation causes the mechanical opening of the channel gate. The time constant of SK channel activation is approximately 5 ms. When calcium levels are depleted, the time constant for channel deactivation ranges from 15–60 ms.