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How accelerated Golgi trafficking may drive Alzheimer's disease (comment on DOI 10.1002/bies.201400116)﻿

In their Hypothesis article Joshi and Wang [1] convincingly argue that Golgi fragmentation accelerates production of Alzheimer’s disease (AD) Ab amyloid (Ab) and that this impacts neuronal function. Indeed, the accumulation of toxic Ab aggregates in the brain is the primary culprit in AD. Ab is derived from sequential cleavage of the amyloid precursor protein (APP) by BABCE1 and g-secretase, and a prerequisite to its formation is the cellular colocalisation of APP with these amyloidogenic endoproteinases [2]. Considering that the Golgi is the hub where APP and the ADrelated secretases transit and are sorted into various cellular compartments, defects in Golgi integrity might be expected to contribute to AD pathology. Eukaryotic cells possess sophisticated machinery that assembles and delivers secretory and membrane proteins to their destination. After synthesis, folding, and partial glycosylation in the endoplasmic reticulum, these proteins traffic through the Golgi apparatus, a complex stack of communicating membranes where their full maturation is achieved and where they are packaged into selected vesicles either for delivery to the plasma membrane, or storage into secretory vesicles, or despatching to the endosomal/lysosomal compartment [3]. APP, BACE1 and g-secretase are integral membrane