Tau fragmentation, aggregation and clearance: the dual role of lysosomal processing.

By Yi-peng Wang, Marta Martínez-Vicente, U. Krüger, Susmita Kaushik, Esther Wong, E. Mandelkow, A. Cuervo. Human Molecular Genetics, 2009

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Tau Protein Hyperphosphorylation and Aggregation in Alzheimer’s Disease and Other Tauopathies, and Possible Neuroprotective Strategies (2016, background): “The truncated core tau unit of the PHF has also been termed “the F3 fragment” (Figure 5) [156].”
Biochemistry and cell biology of tau protein in neurofibrillary degeneration. (2012, background): “Finally, an inducible cell model of Tau aggregation revealed a complex cleavage pattern whereby a cytosolic protease with thrombin-like characteristics cooperates with a lysosomal protease (cathepsin L) to generate a fragment S258–I360 with a high propensity for aggregation, sufficient to nucleate a”
Decoding Alzheimer's disease from perturbed cerebral glucose metabolism: implications for diagnostic and therapeutic strategies. (2013, background): “Some investigators proposed a two-hit hypothesis to explain the role of oxidative stress in AD pathology (Wang et al., 2009a).”
Autophagy and Neurodegeneration: Pathogenic Mechanisms and Therapeutic Opportunities. (2017, neutral): “Tau has also been shown to bind lysosomal membranes and impair lysosomal permeability in vitro and in a mouse model of AD (Collin et al., 2014; Wang et al., 2009).”