Evidence map›Paper›PMID 23603909›Full record

ArticleThe Journal of biological chemistry2013

Ubiquitin-specific protease 7 is a regulator of ubiquitin-conjugating enzyme UbE2E1.

Feroz Sarkari, Keith Wheaton, Anthony La Delfa, Majda Mohamed, Faryal Shaikh, Rahima Khatun, Cheryl H Arrowsmith, Lori Frappier, Vivian Saridakis, Yi Sheng

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed, 1 pooled it
2.1field-weighted citation impact, top 13% 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

28 citing papers in PubMed, 1 synthesis or guideline pooled it, 46 citations in OpenAlex.

  1. Pooled it
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  4. Review
  5. Article
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  7. Article
  8. Article
  9. Review
  10. Molecular Mechanisms of DUBs Regulation in Signaling and Disease.International journal of molecular sciences · 2021
    Review
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  12. Article
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  15. Article
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  18. Article
  19. UbE2E1/UBCH6 Is a CriticalThe Journal of biological chemistry · 2017
    Article
  20. Article
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

10 authors at 3 institutions in 2 countries.

Feroz SarkariDepartment of Biology, York University, Toronto, Ontario M3J 1P3.
Keith WheatonDepartment of Biology, York University, Toronto, Ontario M3J 1P3.
Anthony La DelfaDepartment of Biology, York University, Toronto, Ontario M3J 1P3.
Majda MohamedDepartment of Biology, York University, Toronto, Ontario M3J 1P3.
Faryal ShaikhDepartment of Biology, York University, Toronto, Ontario M3J 1P3.
Rahima KhatunDepartment of Biology, York University, Toronto, Ontario M3J 1P3.
Cheryl H ArrowsmithDivision of Cancer Genomics and Proteomics, Ontario Cancer Institute, University Health Network, Toronto, Ontario M5G 1L7.
Lori FrappierDepartment of Molecular Genetics, University of Toronto, Toronto, Ontario M5S 1A8, Canada.
Vivian SaridakisDepartment of Biology, York University, Toronto, Ontario M3J 1P3. Electronic address: vsaridak@yorku.ca.
Yi ShengDepartment of Biology, York University, Toronto, Ontario M3J 1P3. Electronic address: yisheng@yorku.ca.
York University · CAUniversity Health Network · CAUniversity of Toronto · CA

Funding

Canadian Institutes of Health Research 106583
6 · The paper itself

Abstract

Ubiquitin-specific protease 7 (USP7) is a deubiquitinating enzyme found in all eukaryotes that catalyzes the removal of ubiquitin from specific target proteins. Here, we report that UbE2E1, an E2 ubiquitin conjugation enzyme with a unique N-terminal extension, is a novel USP7-interacting protein. USP7 forms a complex with UbE2E1 in vitro and in vivo through the ASTS USP7 binding motif within its N-terminal extension in an identical manner with other known USP7 binding proteins. We show that USP7 attenuates UbE2E1-mediated ubiquitination, an effect that requires the N-terminal ASTS sequence of UbE2E1 as well as the catalytic activity of USP7. Additionally, USP7 is critical in maintaining the steady state levels of UbE2E1 in cells. This study reveals a new cellular mechanism that couples the opposing activities of the ubiquitination machinery and a deubiquitinating enzyme to maintain and modulate the dynamic balance of the ubiquitin-proteasome system.

Indexed as

Amino Acid MotifsHeLa CellsHumansProteasome Endopeptidase ComplexProtein BindingUbiquitinationUbiquitin-Conjugating EnzymesUbiquitin-Specific Peptidase 7Ubiquitin ThiolesteraseProteasome Endopeptidase ComplexUBE2E1 protein, humanUbiquitin-Conjugating EnzymesUbiquitin-Specific Peptidase 7Ubiquitin ThiolesteraseUSP7 protein, humanDeubiquitinationE3 Ubiquitin LigaseProtein StructureUbiquitinationUbiquitin-conjugating Enzyme (Ubc)

Identifiers

PMID23603909
PMCPMC3675629
OpenAlexW1980936182

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.