Publikation: Degradation of FAT10 by the 26S proteasome is independent of ubiquitylation but relies on NUB1L
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2009
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FEBS Letters. 2009, 583(3), pp. 591-594. ISSN 0014-5793. eISSN 1873-3468. Available under: doi: 10.1016/j.febslet.2009.01.006
Zusammenfassung
The ubiquitin-like modifier FAT10 targets proteins for degradation by the proteasome, a process accelerated by the UBL-UBA domain protein NEDD8 ultimate buster 1-long. Here, we show that FAT10-mediated degradation occurs independently of poly-ubiquitylation as purified 26S proteasome readily degraded FAT10-dihydrofolate reductase (DHFR) but not ubiquitin-DHFR in vitro. Interestingly, the 26S proteasome could only degrade FAT10-DHFR when NUB1L was present. Knock-down of NUB1L attenuated the degradation of FAT10-DHFR in intact cells suggesting that NUB1L determines the degradation rate of FAT10-linked proteins. In conclusion, our data establish FAT10 as a ubiquitin-independent but NUB1L-dependent targeting signal for proteasomal degradation.
Zusammenfassung in einer weiteren Sprache
Fachgebiet (DDC)
570 Biowissenschaften, Biologie
Schlagwörter
Ubiquitin, FAT10, 26S proteasome, NUB1L, Degradation
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SCHMIDTKE, Gunter, Birte KALVERAM, Marcus GRÖTTRUP, 2009. Degradation of FAT10 by the 26S proteasome is independent of ubiquitylation but relies on NUB1L. In: FEBS Letters. 2009, 583(3), pp. 591-594. ISSN 0014-5793. eISSN 1873-3468. Available under: doi: 10.1016/j.febslet.2009.01.006BibTex
@article{Schmidtke2009Degra-1188,
year={2009},
doi={10.1016/j.febslet.2009.01.006},
title={Degradation of FAT10 by the 26S proteasome is independent of ubiquitylation but relies on NUB1L},
number={3},
volume={583},
issn={0014-5793},
journal={FEBS Letters},
pages={591--594},
author={Schmidtke, Gunter and Kalveram, Birte and Gröttrup, Marcus}
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