The memory dysfunctions that characterize Alzheimer's disease (AD) are strongly correlated with synapse loss. The amyloid precursor protein (APP) and its cleavage product Aβ play central roles in synapse and memory loss, and thus are strongly implicated in the pathogenesis of AD. Numerous in vitro and transgenic AD mouse model studies have shown that overexpression of APP leads to Aβ accumulation, which causes decreased synaptic activity and dendritic spine density. However, the normal synaptic function of APP itself is not fully understood. Several recent studies have found that full-length APP promotes synaptic activity, synapse formation, and dendritic spine formation. These findings cast APP as a potential key player in learning and memory. It is of interest that the synaptic functions of full-length APP are opposite to the effects associated with pathological Aβ accumulation. In this review, we will summarize the normal functions of APP at synapses and spines along with other known functions of APP, including its role in cell motility, neuronal migration, and neurite outgrowth. These studies shed light on the physiological actions of APP, independent of Aβ effects, and thus lead to a better understanding of the synaptic dysfunctions associated with AD.