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The CUE domain of Cue1 aligns growing ubiquitin chains with Ubc7 for rapid elongation

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Official URL:https://doi.org/10.1016/j.molcel.2016.04.031
PubMed:View item in PubMed
Creators Name:von Delbrueck, M. and Kniss, A. and Rogov, V.V. and Pluska, L. and Bagola, K. and Loehr, F. and Guentert, P. and Sommer, T. and Doetsch, V.
Journal Title:Molecular Cell
Journal Abbreviation:Mol Cell
Volume:62
Number:6
Page Range:918-928
Date:16 June 2016
Abstract:Ubiquitin conjugation is an essential process modulating protein function in eukaryotic cells. Surprisingly, little is known about how the progressive assembly of ubiquitin chains is managed by the responsible enzymes. Only recently has ubiquitin binding activity emerged as an important factor in chain formation. The Ubc7 activator Cue1 carries a ubiquitin binding CUE domain that substantially stimulates K48-linked polyubiquitination mediated by Ubc7. Our results from NMR-based analysis and in vitro ubiquitination reactions point out that two parameters accelerate ubiquitin chain assembly: the increasing number of CUE binding sites and the position of CUE binding within a growing chain. In particular, interactions with a ubiquitin moiety adjacent to the acceptor ubiquitin facilitate chain elongation. These data indicate a mechanism for ubiquitin binding in which Cue1 positions Ubc7 and the distal acceptor ubiquitin for rapid polyubiquitination. Disrupting this mechanism results in dysfunction of the ERAD pathway by a delayed turnover of substrates.
ISSN:1097-2765
Publisher:Cell Press / Elsevier (U.S.A.)
Item Type:Article

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