Evidence map›Paper›PMID 28475037›Full record

ArticleeLife2017

SENP8 limits aberrant neddylation of NEDD8 pathway components to promote cullin-RING ubiquitin ligase function.

Kate E Coleman, Miklós Békés, Jessica R Chapman, Sarah B Crist, Mathew Jk Jones, Beatrix M Ueberheide, Tony T Huang

Open access · goldAbstract read
In one paragraph

Article in eLife, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
2.5field-weighted citation impact, top 10% 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

31 citing papers in PubMed, 47 citations in OpenAlex.

  1. Review
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  3. Article
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  9. Article
  10. Protein neddylation and its role in health and diseases.Signal transduction and targeted therapy · 2024
    Review
  11. Article
  12. Review
  13. Review
  14. Article
  15. Article
  16. Neddylation is critical to cortical development by regulating Wnt/β-catenin signaling.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  17. Review
  18. Review
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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

7 authors at 2 institutions in 1 country.

Kate E ColemanDepartment of Biochemistry and Molecular Pharmacology, New York University School of Medicine, New York, United States.ORCID 0000-0003-4676-4981
Miklós BékésDepartment of Biochemistry and Molecular Pharmacology, New York University School of Medicine, New York, United States.
Jessica R ChapmanProteomics Laboratory, Division of Advanced Research Technologies, New York University School of Medicine, New York, United States.
Sarah B CristDepartment of Biochemistry and Molecular Pharmacology, New York University School of Medicine, New York, United States.
Mathew Jk JonesMolecular Biology Program, Sloan Kettering Institute, Memorial Sloan Kettering Cancer Center, New York, Unites States.
Beatrix M UeberheideDepartment of Biochemistry and Molecular Pharmacology, New York University School of Medicine, New York, United States.
Tony T HuangDepartment of Biochemistry and Molecular Pharmacology, New York University School of Medicine, New York, United States.ORCID 0000-0001-9291-5002
New York University · USMemorial Sloan Kettering Cancer Center · US

Funding

Vaccine FacilityP30CA016087 · NCI · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI ADRIANA HEGUY · 1985 to 2026
$83.1M
Mechanisms of reversible DUB oxidation in genome stability pathways - RevisionR01ES025166 · NIEHS · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI HUANG, TONY TUNG · 2015 to 2020
$2.3M
The Regulation of DNA Repair by Anchored and Unanchored Ubiquitin ChainsF32GM100598 · NIGMS · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI BEKES, MIKLOS · 2012 to 2015
$194k
NCI NIH HHS P30 CA016087NIEHS NIH HHS R01 ES025166NIGMS NIH HHS F32 GM100598
6 · The paper itself

Abstract

NEDD8 is a ubiquitin-like modifier most well-studied for its role in activating the largest family of ubiquitin E3 ligases, the cullin-RING ligases (CRLs). While many non-cullin neddylation substrates have been proposed over the years, validation of true NEDD8 targets has been challenging, as overexpression of exogenous NEDD8 can trigger NEDD8 conjugation through the ubiquitylation machinery. Here, we developed a deconjugation-resistant form of NEDD8 to stabilize the neddylated form of cullins and other non-cullin substrates. Using this strategy, we identified Ubc12, a NEDD8-specific E2 conjugating enzyme, as a substrate for auto-neddylation. Furthermore, we characterized SENP8/DEN1 as the protease that counteracts Ubc12 auto-neddylation, and observed aberrant neddylation of Ubc12 and other NEDD8 conjugation pathway components in SENP8-deficient cells. Importantly, loss of SENP8 function contributes to accumulation of CRL substrates and defective cell cycle progression. Thus, our study highlights the importance of SENP8 in maintaining proper neddylation levels for CRL-dependent proteostasis.

Indexed as

Protein Processing, Post-TranslationalCell CycleEndopeptidasesGene Expression RegulationHEK293 CellsHeLa CellsHumansNEDD8 ProteinUbiquitin-Conjugating EnzymesEndopeptidasesNEDD8 ProteinNEDD8 protein, humanSENP8 protein, humanUBE2M protein, humanUbiquitin-Conjugating EnzymesbiochemistryCRLhumanNedd8Ubc12ubiquitinUbl protease

Identifiers

PMID28475037
PMCPMC5419743
OpenAlexW2610197482

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.