Evidence map›Paper›PMID 10637223›Full record

ArticleThe EMBO journal2000

Monoubiquitin carries a novel internalization signal that is appended to activated receptors.

S C Shih, K E Sloper-Mould, L Hicke

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 98 papers.

0numbers the graph read from it
0cells of the map it votes in
98citing papers in PubMed
13.0field-weighted citation impact, top 1% of its field
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

98 citing papers in PubMed, 286 citations in OpenAlex.

  1. Review
  2. Review
  3. The Molecular Toolbox for Linkage Type-Specific Analysis of Ubiquitin Signaling.Chembiochem : a European journal of chemical biology · 2025
    Review
  4. Article
  5. Article
  6. Fast friends - Ubiquitin-like modifiers as engineered fusion partners.Seminars in cell & developmental biology · 2022
    Review
  7. E2Computers in biology and medicine · 2022
    Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Article

38 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

3 authors at 1 institution in 1 country.

S C ShihDepartment of Biochemistry, Molecular Biology and Cell Biology, Northwestern University, Evanston, IL 60208, USA.
K E Sloper-Mould
L Hicke
Northwestern University · US

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
NIDDK NIH HHS DK53257NIDDK NIH HHS R01 DK053257NIGMS NIH HHS T32 GM008061NIGMS NIH HHS T32GM08061
6 · The paper itself

Abstract

Ubiquitin modification of signal transducing receptors at the plasma membrane is necessary for rapid receptor internalization and downregulation. We have investigated whether ubiquitylation alters a receptor cytoplasmic tail to reveal a previously masked internalization signal, or whether ubiquitin itself carries an internalization signal. Using an alpha-factor receptor-ubiquitin chimeric protein, we demonstrate that monoubiquitin can mediate internalization of an activated receptor that lacks all cytoplasmic tail sequences. Furthermore, fusion of ubiquitin in-frame to the stable plasma membrane protein Pma1p stimulates endocytosis of this protein. Ubiquitin does not carry a functional tyrosine- or di-leucine-based internalization signal. Instead, the three-dimensional structure of the folded ubiquitin polypeptide carries an internalization signal that consists of two surface patches surrounding the critical residues Phe4 and Ile44. We conclude that ubiquitin functions as a novel regulated internalization signal that can be appended to a plasma membrane protein to trigger downregulation.

Indexed as

Saccharomyces cerevisiae ProteinsTranscription FactorsAmino Acid SequenceAmino Acid SubstitutionCell MembraneIsoenzymesIsoleucineKineticsModels, MolecularMolecular Sequence DataMutagenesis, Site-DirectedPhenylalanineProtein ConformationProton-Translocating ATPasesReceptors, Mating FactorReceptors, PeptideIsoenzymesIsoleucinePhenylalaninePMA1 protein, S cerevisiaePMA2 protein, S cerevisiaeProton-Translocating ATPasesReceptors, Mating FactorReceptors, PeptideRecombinant Fusion ProteinsSaccharomyces cerevisiae ProteinsTranscription FactorsUbiquitins

Identifiers

PMID10637223
PMCPMC305553
OpenAlexW2153991959

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.