Abstract
Background: Ubiquitin-modified TDP-43 protein aggregates characterize common neurodegenerative diseases. Results: UBE2E ubiquitin-conjugating enzymes and ubiquitin isopeptidase Y (UBPY) are functional interactors of TDP-43 in cell culture and fly models. Conclusion: Specific regulators of TDP-43 ubiquitination influence its aggregation and neurotoxic properties. Significance: UBE2E and UBPY enzymes may modulate the course of TDP-43 diseases. © 2014 by The American Society for Biochemistry and Molecular Biology, Inc.
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CITATION STYLE
Hans, F., Fiesel, F. C., Strong, J. C., Jackel, S., Rasse, T. M., Geisler, S., … Kahle, P. J. (2014). UBE2E ubiquitin-conjugating enzymes and ubiquitin isopeptidase y regulate TDP-43 protein ubiquitination. Journal of Biological Chemistry, 289(27), 19164–19179. https://doi.org/10.1074/jbc.M114.561704
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