Trafficking regulation of proteins in Alzheimer's disease - PubMed (original) (raw)
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Trafficking regulation of proteins in Alzheimer's disease
Shangtong Jiang et al. Mol Neurodegener. 2014.
Abstract
The β-amyloid (Aβ) peptide has been postulated to be a key determinant in the pathogenesis of Alzheimer's disease (AD). Aβ is produced through sequential cleavage of the β-amyloid precursor protein (APP) by β- and γ-secretases. APP and relevant secretases are transmembrane proteins and traffic through the secretory pathway in a highly regulated fashion. Perturbation of their intracellular trafficking may affect dynamic interactions among these proteins, thus altering Aβ generation and accelerating disease pathogenesis. Herein, we review recent progress elucidating the regulation of intracellular trafficking of these essential protein components in AD.
Figures
Figure 1
Typical trafficking route of APP, BACE1, α-secretase and γ-secretase. Newly synthesized APP, BACE1, α-secretase and γ-secretase traffic through the secretory pathway, from the ER to Golgi/TGN and to the plasma membrane, during which process retrieval may occur and APP may be cleaved to generate Aβ. At the plasma membrane APP is largely subjected to non-amyloidogenic processing by α-secretase to release sAPPα. Un-cleaved APP and various secretases at the plasma membrane may undergo endocytosis via early endosome to late endosome/lysosome for degradation. Acidic endosome/lysosome provides optimal environment for BACE1 activity and APP is mainly subjected to amyloidogenic processing for Aβ production in these compartments. In addition, a fraction of these proteins in endosome can be either recycled back to plasma membrane or retrieved back to TGN.
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