p(HGNC:MAPT, pmod(UbK48))
Otub1 displayed strong preference for disassembling Lys48-linked polyubiquitin chains, while leaving Lys63-linked polyubiquitin chains unaffected (Fig. 5a). PubMed:28083634
Conversely, AAV-driven expression of N-terminally truncated Otub1 significantly decreased Lys48-linked polyubiquitin chains of Tau (Fig. 5b), demonstrating that the N-terminal domain of Otub1, which is crucial for its noncanonical role, is not involved in regulation of Tau ubiquitination. PubMed:28083634
Analysis of a catalytically dead mutant with a C91A mutation revealed no effect on Lys48-linked polyubiquitination of Tau PubMed:28083634
Tau is known to be ubiquitylated through Lys48 linkages by CHIP for proteasomal degradation PubMed:26631930
BEL Commons is developed and maintained in an academic capacity by Charles Tapley Hoyt and Daniel Domingo-Fernández at the Fraunhofer SCAI Department of Bioinformatics with support from the IMI project, AETIONOMY. It is built on top of PyBEL, an open source project. Please feel free to contact us here to give us feedback or report any issues. Also, see our Publishing Notes and Data Protection information.
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.