These results implicate Pin1 as a possible modulator of stress-induced NF-H phosphorylation as seen in neurodegenerative disorders like AD and amyotrophic lateral sclerosis.
We have confirmed the involvement of specific proteins previously associated with ALS (Galectin 2 (<i>LGALS3</i>), Transthyretin (<i>TTR</i>), Protein S100-A6 (<i>S100A6</i>), and Protein S100-A11 (<i>S100A11</i>)) and have shown the involvement of proteins not previously described in the ALS context (Methanethiol oxidase (<i>SELENBP1</i>), Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (<i>PIN-1</i>), Calcyclin-binding protein (<i>CACYBP</i>) and Rho-associated protein kinase 2 (<i>ROCK2</i>)).
This study highlights a novel signaling role of PP2A by Pin1 and implicates Pin1 as a therapeutic target to reduce aberrant phosphorylation of NF proteins in neurodegenerative disorders such as AD, PD, and ALS.