Most of early-onset forms of Alzheimer's disease (AD) are caused by inherited mutations located on chromosomes 14 and 1, the gene products of which have been recently identified and referred to as presenilins 1 (PS1) and 2 (PS2), respectively. The first phenotypic alterations triggered by mutated PS were reported to be an increased production of the amyloid peptide (Abeta) and, more precisely, its 42 amino-acids long counterpart Abeta42. This overproduction is thought to be responsible for the genesis of the senile plaques that invade the cortical and subcortical areas of these AD-affected brains. The discovery of PSs has triggered numerous studies aimed at better understanding their normal physiology and the dysfunctions brought by the mutations that could explain, at least in part, the neurodegenerative process taking place in this syndrome. In this review, I will focus on the structural aspects of PS and on the various posttranscriptional events they undergo. I will also briefly discuss that current hypotheses concerning their normal functions and the influence of FAD-linked mutations.