Evidence map›Paper›PMID 25605328›Full record

ArticleMolecular and cellular biology2015

USP7 cooperates with SCML2 to regulate the activity of PRC1.

Emilio Lecona, Varun Narendra, Danny Reinberg

Erratum issuedOpen access · bronzeAbstract read
In one paragraph

Article in Molecular and cellular biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
3.9field-weighted citation impact, top 6% 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

33 citing papers in PubMed, 61 citations in OpenAlex.

  1. Article
  2. Small-molecule allosteric activator of ubiquitin-specific protease 7 (USP7).Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Review
  16. Review
  17. Article
  18. Review
  19. Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

3 authors at 2 institutions in 1 country.

Emilio LeconaHoward Hughes Medical Institute, Department of Biochemistry, New York University School of Medicine, New York, New York, USA.
Varun NarendraHoward Hughes Medical Institute, Department of Biochemistry, New York University School of Medicine, New York, New York, USA.
Danny ReinbergHoward Hughes Medical Institute, Department of Biochemistry, New York University School of Medicine, New York, New York, USA Danny.Reinberg@nyumc.org.
New York University · USHoward Hughes Medical Institute · US

Funding

Vaccine FacilityP30CA016087 · NCI · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI ADRIANA HEGUY · 1985 to 2026
$83.1M
Initiation of Transcription of Protein Coding GenesR37GM037120 · NIGMS · UNIV OF MED/DENT NJ-R W JOHNSON MED SCH · PI REINBERG, DANNY · 2004 to 2013
$4.5M
Transcription Regulation by NC2R01GM064844 · NIGMS · UNIV OF MED/DENT NJ-R W JOHNSON MED SCH · PI REINBERG, DANNY · 2002 to 2014
$3.3M
INITIATION OF TRANSCRIPTION OF PROTEIN CODING GENESR01GM037120 · NIGMS · UNIV OF MED/DENT NJ-R W JOHNSON MED SCH · PI REINBERG, DANNY F · 1986 to 2001
$634k
A Mass Spectrometry System for Quantitative ProteomicsS10OD016400 · OD · RBHS-ROBERT WOOD JOHNSON MEDICAL SCHOOL · PI LOBEL, PETER · 2014 to 2014
$561k
Howard Hughes Medical InstituteNCI NIH HHS P30 CA016087NIGMS NIH HHS GM064844NIGMS NIH HHS GM37120NIGMS NIH HHS R01 GM037120NIGMS NIH HHS R01 GM064844NIGMS NIH HHS R37 GM037120NIH HHS S10 OD016400
6 · The paper itself

Abstract

USP7 is a protein deubiquitinase with an essential role in development. Here, we provide evidence that USP7 regulates the activity of Polycomb repressive complex 1 (PRC1) in coordination with SCML2. There are six versions of PRC1 defined by the association of one of the PCGF homologues (PCGF1 to PCGF6) with the common catalytic subunit RING1B. First, we show that SCML2, a Polycomb group protein that associates with PRC1.2 (containing PCGF2/MEL18) and PRC1.4 (containing PCGF4/BMI1), modulates the localization of USP7 and bridges USP7 with PRC1.4, allowing for the stabilization of BMI1. Chromatin immunoprecipitation (ChIP) experiments demonstrate that USP7 is found at SCML2 and BMI1 target genes. Second, inhibition of USP7 leads to a reduction in the level of ubiquitinated histone H2A (H2Aub), the catalytic product of PRC1 and key for its repressive activity. USP7 regulates the posttranslational status of RING1B and BMI1, a specific component of PRC1.4. Thus, not only does USP7 stabilize PRC1 components, its catalytic activity is also necessary to maintain a functional PRC1, thereby ensuring appropriate levels of repressive H2Aub.

Indexed as

Cell LineHumansPolycomb-Group ProteinsPolycomb Repressive Complex 1Protein Interaction MapsUbiquitin-Specific Peptidase 7Ubiquitin ThiolesterasePolycomb-Group ProteinsPolycomb Repressive Complex 1SCML2 protein, humanUbiquitin-Specific Peptidase 7Ubiquitin ThiolesteraseUSP7 protein, human

Identifiers

PMID25605328
PMCPMC4355532
OpenAlexW2142795372

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.