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

doi:10.1074/jbc.M114.561704

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

Neuroscience

Research output: Contribution to journal › Article › peer-review

40 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 language	English (US)
Pages (from-to)	19164-19179
Number of pages	16
Journal	Journal of Biological Chemistry
Volume	289
Issue number	27
DOIs	https://doi.org/10.1074/jbc.M114.561704
State	Published - Jul 4 2014

ASJC Scopus subject areas

Biochemistry
Molecular Biology
Cell Biology

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title = "UBE2E ubiquitin-conjugating enzymes and ubiquitin isopeptidase y regulate TDP-43 protein ubiquitination",

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.",

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doi = "10.1074/jbc.M114.561704",

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T1 - UBE2E ubiquitin-conjugating enzymes and ubiquitin isopeptidase y regulate TDP-43 protein ubiquitination

AU - Hans, Friederike

AU - Fiesel, Fabienne C.

AU - Strong, Jennifer C.

AU - Jackel, Sändra

AU - Rasse, Tobias M.

AU - Geisler, Sven

AU - Springer, Wolfdieter

AU - Schulz, Jörg B.

AU - Voigt, Aaron

AU - Kahle, Philipp J.

PY - 2014/7/4

Y1 - 2014/7/4

N2 - 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.

AB - 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.

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

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