Journal
EMBO JOURNAL
Volume 22, Issue 6, Pages 1273-1281Publisher
WILEY-BLACKWELL
DOI: 10.1093/emboj/cdg140
Keywords
CUE domain; monoubiquitylation; Rsp5; ubiquitin-binding protein; Vps9
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Funding
- NHLBI NIH HHS [HL50121] Funding Source: Medline
- NIDDK NIH HHS [R01 DK053257, DK53257] Funding Source: Medline
- NIGMS NIH HHS [T32GM08061, T32 GM008061] Funding Source: Medline
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Monoubiquitylation is a regulatory signal, like phosphorylation, that can alter the activity, location or structure of a protein. Monoubiquitin signals are likely to be recognized by ubiquitin-binding proteins that transmit the regulatory information conferred by monoubiquitylation. To identify monoubiquitin-binding proteins, we used a mutant ubiquitin that lacks the primary site of polyubiquitin chain formation as bait in a two-hybrid screen. The C-terminus of Vps9, a protein required in the yeast endocytic pathway, interacted specifically with monoubiquitin. The region required for monoubiquitin binding mapped to the Vps9 CUE domain, a sequence previously identified by database searches as similar to parts of the yeast Cue1 and mammalian Tollip proteins. We demonstrate that CUE domains bind directly to monoubiquitin and we have defined crucial interaction surfaces on both binding partners. The Vps9 CUE domain is required to promote monoubiquitylation of Vps9 by the Rsp5 hect domain ubiquitin ligase. Thus, we conclude that the CUE motif is an evolutionarily conserved monoubiquitin-binding domain that mediates intramolecular monoubiquitylation.
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