UBE2E ubiquitin-conjugating enzymes and ubiquitin isopeptidase y regulate TDP-43 protein ubiquitination

Friederike Hans, Fabienne C. Fiesel, Jennifer C. Strong, Sändra Jackel, Tobias M. Rasse, Sven Geisler, Wolfdieter Springer, Jörg B. Schulz, Aaron Voigt, Philipp J. Kahle

Research output: Contribution to journalArticle

35 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)19164-19179
Number of pages16
JournalJournal of Biological Chemistry
Volume289
Issue number27
DOIs
StatePublished - Jul 4 2014

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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    Hans, F., Fiesel, F. C., Strong, J. C., Jackel, S., Rasse, T. M., Geisler, S., Springer, W., Schulz, J. B., Voigt, A., & 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