Publikation:

Ubiquitin binding by a CUE domain regulates ubiquitin chain formation by ERAD E3 ligases

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2013

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Bagola, Katrin
Dellbrück, Maximilian von
Dittmar, Gunnar
Ziv, Inbal
Glickman, Michael H.
Ciechanover, Aaron
Sommer, Thomas

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http://nbn-resolving.de/urn:nbn:de:bsz:352-251305
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https://doi.org/10.1016/j.molcel.2013.04.005
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Published

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Molecular Cell. 2013, 50(4), pp. 528-539. ISSN 1097-2765. eISSN 1097-4164. Available under: doi: 10.1016/j.molcel.2013.04.005

Zusammenfassung

Ubiquitin-binding domains (UBDs) differentially recognize ubiquitin (ub) modifications. Some of them specifically bind mono-ub, as has been shown for the CUE domain. Interestingly, so far no significant ubiquitin binding has been observed for the CUE domain of yeast Cue1p. Cue1p is receptor and activator of the ubiquitin-conjugating enzyme Ubc7p. It integrates Ubc7p into endoplasmic reticulum (ER) membrane-bound ubiquitin ligase complexes, and thus, it is crucial for ER-associated protein degradation (ERAD). Here we show that the CUE domain of Cue1p binds ubiquitin chains, which is pivotal for the efficient formation of K48-linked polyubiquitin chains in vitro. Mutations that abolish ubiquitin binding by Cue1p affect the turnover of ERAD substrates in vivo. Our data strongly imply that the CUE domain facilitates substrate ubiquitylation by stabilizing growing ubiquitin chains at the ERAD ubiquitin ligases. Hence, we demonstrate an unexpected function of a UBD in the regulation of ubiquitin chain synthesis.

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570 Biowissenschaften, Biologie

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ISO 690BAGOLA, Katrin, Maximilian von DELLBRÜCK, Gunnar DITTMAR, Martin SCHEFFNER, Inbal ZIV, Michael H. GLICKMAN, Aaron CIECHANOVER, Thomas SOMMER, 2013. Ubiquitin binding by a CUE domain regulates ubiquitin chain formation by ERAD E3 ligases. In: Molecular Cell. 2013, 50(4), pp. 528-539. ISSN 1097-2765. eISSN 1097-4164. Available under: doi: 10.1016/j.molcel.2013.04.005
BibTex
@article{Bagola2013-05-23Ubiqu-25130,
  year={2013},
  doi={10.1016/j.molcel.2013.04.005},
  title={Ubiquitin binding by a CUE domain regulates ubiquitin chain formation by ERAD E3 ligases},
  number={4},
  volume={50},
  issn={1097-2765},
  journal={Molecular Cell},
  pages={528--539},
  author={Bagola, Katrin and Dellbrück, Maximilian von and Dittmar, Gunnar and Scheffner, Martin and Ziv, Inbal and Glickman, Michael H. and Ciechanover, Aaron and Sommer, Thomas}
}
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