The presence of amyloid beta (Aβ) protein deposits in neuronal extracellular space is one of the hallmarks of Alzheimer's disease. The role of ApoER2 in Alzheimer's disease is relevant, yet incompletely understood. New evidence suggests ApoER2 plays a major role in the regulation of amyloid-β formation in the brain. The amyloid-β peptide is derived from the cleavage of APP by gamma secretase. ApoER2 works to reduce APP trafficking by altering break down. This interaction decreases APP endocytosis leading to an increase in amyloid-β production. In addition, the expression of ApoER2 within intracellular compartments leads to increased gamma secretase activity, a protease which works to cleave APP into Aβ.