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First published online 14 April 2009
doi: 10.1242/jcs.044255

Journal of Cell Science 122, 1374-1381 (2009)
Published by The Company of Biologists 2009
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Research Article

A Ubc7p-binding domain in Cue1p activates ER-associated protein degradation

Zlatka Kostova, Jennifer Mariano, Simone Scholz, Carolin Koenig and Allan M. Weissman*

Laboratory of Protein Dynamics and Signaling, Center for Cancer Research, National Cancer Institute, Frederick, MD 21702, USA

* Author for correspondence (e-mail: amw{at}nih.gov)

Accepted 20 January 2009

Cue1p is an N-terminally anchored endoplasmic reticulum (ER) protein essential for the activity of the two major yeast RING finger ubiquitin ligases (E3s) implicated in ER-associated degradation (ERAD). Cue1p contains a CUE domain, which for several proteins is known to bind ubiquitin. We now establish that the CUE domain is dispensable for ERAD of substrates of both Hrd1p and Doa10p and that the Cue1p transmembrane domain is similarly not required for degradation of the Hrd1p substrate CPY*. Cue1p interacts with the ERAD E2 Ubc7p in vivo. We show that a discrete C-terminal Ubc7p binding region (U7BR) of Cue1p is required for ERAD and for Ubc7p-dependent ubiquitylation by Hrd1p in vitro. Strikingly, when Ubc7p is stabilized by direct anchoring to the ER membrane, the U7BR is sufficient to restore ERAD in cells lacking Cue1p. Thus, discrete E2 binding sites independent of ubiquitin ligase domains have the potential to activate ubiquitylation.

Key words: ER-associated degradation, Proteasome, Ubiquitin, S. cerevisiae, CUE1, UBC7


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© The Company of Biologists Ltd 2009