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Nat. Rev. Neurol. doi:10.1038/nrneurol.2017.99 Figure 4 Mechanisms that trigger ER stress in neurodegenerative disease Figure 4 | Mechanisms that trigger ER stress in neurodegenerative disease. Correctly folded proteins are processed in the endoplasmic reticulum (ER) and trafficked to the Golgi apparatus for further maturation and distribution to their final destination. Protein folding and maturation at the ER is altered in neurodegenerative disease owing to the effects of protein aggregates on various mechanisms, which include inhibition of protein folding by inhibiting chaperones, interference with the ER-associated degradation pathway, perturbation of ER-to-Golgi trafficking, inhibition of proximal unfolded protein response components, and exacerbation of ER calcium release. ERAD, ER-associated degradation; FUS, fused in sarcoma; PDI, protein disulfide isomerase; SOD1, superoxide dismutase 1; VAPB, vesicle-associated membrane protein-associated protein B. Hetz, C. & Saxena, S. (2017) ER stress and the unfolded protein response in neurodegeneration Nat. Rev. Neurol. doi:10.1038/nrneurol.2017.99