Evidence map›Paper›PMID 12628920›Full record

ArticleThe EMBO journal2003

A ubiquitin-binding motif required for intramolecular monoubiquitylation, the CUE domain.

Susan C Shih, Gali Prag, Smitha A Francis, Myra A Sutanto, James H Hurley, Linda Hicke

Abstract read
In one paragraph

Article in The EMBO journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 118 papers.

0numbers the graph read from it
0cells of the map it votes in
118citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

118 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Journal of fungi (Basel, Switzerland) · 2025
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. A context-dependent and disordered ubiquitin-binding motif.Cellular and molecular life sciences : CMLS · 2022
    Article
  12. Article
  13. Cells · 2022
    Article
  14. Review
  15. Article
  16. Article
  17. Ubiquitination in the ERAD Process.International journal of molecular sciences · 2020
    Review
  18. Article
  19. Review
  20. Article

58 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors.

Susan C ShihDepartment of Biochemistry, Molecular Biology and Cell Biology, Northwestern University, Evanston, IL 60208-3500, USA.
Gali Prag
Smitha A Francis
Myra A Sutanto
James H Hurley
Linda Hicke

Funding

CELLULAR &MOLECULAR BASIS OF DISEASE TRAINING PROGRAMT32GM008061 · NIGMS · NORTHWESTERN UNIVERSITY · PI CARTHEW, RICHARD W. · 1985 to 2022
$17.1M
UBIQUITIN-DEPENDENT ENDOCYTOSIS OF SIGNALING RECEPTORSR01DK053257 · NIDDK · NORTHWESTERN UNIVERSITY · PI HICKE, LINDA A. · 1998 to 2010
$2.5M
REGULATION OF M2 MUSCARINIC RECEPTORS BY PHOSPHORYLATIONR01HL050121 · NHLBI · NORTHWESTERN UNIVERSITY · PI HICKE, LINDA A. · 1994 to 2001
$529k
Structural Biology /Structural Genomics of TraffickingZ01DK036118 · NIDDK · DIABETES, DIGESTIVE, KIDNEY DISEASES · PI HURLEY, JAMES H · 1994 to 2006
–
NHLBI NIH HHS HL50121NIDDK NIH HHS DK53257NIDDK NIH HHS R01 DK053257NIGMS NIH HHS T32 GM008061NIGMS NIH HHS T32GM08061
6 · The paper itself

Abstract

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.

Indexed as

Vesicular Transport ProteinsAmino Acid MotifsAmino Acid SequenceCarrier ProteinsConserved SequenceEscherichia coliEvolution, MolecularFungal ProteinsGuanine Nucleotide Exchange FactorsMolecular Sequence DataMutationPeptide FragmentsProtein BindingProtein Structure, TertiaryRecombinant ProteinsSaccharomyces cerevisiaeCarrier ProteinsFungal ProteinsGuanine Nucleotide Exchange FactorsPeptide FragmentsRecombinant ProteinsSaccharomyces cerevisiae ProteinsUbiquitinsVesicular Transport ProteinsVPS9 protein, S cerevisiae

Identifiers

PMID12628920
PMCPMC151082

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.