Potassium channels regulate a diverse array of physiological processes, including key aspects of learning and memory. Small-conductance calcium-activated potassium (SK or KCa2) channels are voltage-insensitive K channels that are gated solely by intracellular Ca2+. Functional SK channels are formed through heteromeric complexes of [alpha]-pore-forming subunits and CaM, with which they are constitutively associated. Previous work using a proteomics approach demonstrated that SK2 channels bind protein kinase CK2 (CK2) and protein phosphate 2A (PP2A) to form a macromolecular complex, and that CK2 phosphatase 2A (PP2A) to form a macromolecular complex, and that CK2 phosphorylation of SK2-bound calmodulin (CaM) on threonine 80 (T80) decreases SK channel Ca2+ sensitivity by destabilizing the open state of the channel. The work detailed in this thesis extends these initial findings.