... our work, but one previously proposed explanation is that the reduced affinity of phosphorylated tau for microtubules might trigger its misfolding and secretion through a non-canonical secretory mechanism (Zhang et al., 2021). Previous work has also shown that GSK-3β can phosphorylate α-synuclein...

...Zhao-Feng Li; Lei Cui; Mi-Mi Jin; Dong-Yan Hu; Xiao-Gang Hou; Shu-Shu Liu; Xiong Zhang; Jian-Hong Zhu ABSTRACT Parkinson's disease (PD) is associated with α-synuclein-based Lewy body pathology, which has been difficult to observe in conventional two-dimensional (2D) cell culture and even in animal...

...Cathryn L. Ugalde; Sarah J. Annesley; Shane E. Gordon; Katelyn Mroczek; Matthew A. Perugini; Victoria A. Lawson; Paul R. Fisher; David I. Finkelstein; Andrew F. Hill ABSTRACT The misfolding and aggregation of the largely disordered protein, α-synuclein, is a central pathogenic event that occurs...

... of the lipid-binding SNARE complex component α-synuclein (SNCA) underlies this vulnerability and defines stages of disease progression. Determinants of SNCA levels and mechanisms of SNCA neurotoxicity have been intensely investigated. In view of the physiological roles of SNCA in blood to modulate vesicle...

... by the aggregation of the protein, α-synuclein. This Review discusses current evidence that implicates Ca 2+ in the pathogenesis of Parkinson's disease. Understanding the mechanisms by which Ca 2+ signaling contributes to the progression of this disease will be crucial for the development of effective therapies...

...-43, FUS and α-synuclein, as well as missense mutant versions of these proteins that cause neurodegenerative disease. Potentiated Hsp104 variants also rescue toxicity and aggregation of TAF15 but not EWSR1, two RNA-binding proteins with a prion-like domain that are connected with the development...