Evidences p(HGNC:OTUB1) to p(HGNC:MAPT)

Taken together, our data indicate that Otub1, a deubiquitinating enzyme, is a novel positive regulator of Tau aggregation and Tau stability in vitro, in a nonneuronal cell line.

Otub1 also significantly increased total Tau protein level compared with GFP control (Fig. 3b).

We found that Tau degradation was significantly impaired in primary neurons infected with Otub1 WT, but not with catalytically dead mutant C91A, compared with GFP control.

These results indicate that Otub1 regulates Tau degradation, dependent on its catalytic activity (Fig. 5c).

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If you find BEL Commons useful in your work, please consider citing: Hoyt, C. T., Domingo-Fernández, D., & Hofmann-Apitius, M. (2018). BEL Commons: an environment for exploration and analysis of networks encoded in Biological Expression Language. Database, 2018(3), 1–11.