Evidence map›Paper›PMID 26632597›Full record

ArticleNature communications2015

Gln40 deamidation blocks structural reconfiguration and activation of SCF ubiquitin ligase complex by Nedd8.

Clinton Yu, Haibin Mao, Eric J Novitsky, Xiaobo Tang, Scott D Rychnovsky, Ning Zheng, Lan Huang

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

30 citing papers in PubMed, 43 citations in OpenAlex.

  1. Article
  2. Kinetic principles of chemical cross-link formation for protein-protein interactions.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  3. Review
  4. An expanded lexicon for the ubiquitin code.Nature reviews. Molecular cell biology · 2023
    Review
  5. Article
  6. Article
  7. Review
  8. Article
  9. NEDD8 and ubiquitin ligation by cullin-RING E3 ligases.Current opinion in structural biology · 2021
    Review
  10. Article
  11. Review
  12. Basis for metabolite-dependent Cullin-RING ligase deneddylation by the COP9 signalosome.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  13. Article
  14. Review
  15. Article
  16. Probing HMolecular & cellular proteomics : MCP · 2019
    Article
  17. Article
  18. Article
  19. Review
  20. Review
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 3 institutions in 1 country.

Clinton YuDepartment of Physiology and Biophysics, University of California, Irvine, California 92697, USA.
Haibin MaoDepartment of Pharmacology and Howard Hughes Medical Institute, University of Washington, Seattle, Washington 98195, USA.
Eric J NovitskyDepartment of Chemistry, University of California, Irvine, California 92697, USA.
Xiaobo TangDepartment of Pharmacology and Howard Hughes Medical Institute, University of Washington, Seattle, Washington 98195, USA.
Scott D RychnovskyDepartment of Chemistry, University of California, Irvine, California 92697, USA.
Ning ZhengDepartment of Pharmacology and Howard Hughes Medical Institute, University of Washington, Seattle, Washington 98195, USA.
Lan HuangDepartment of Physiology and Biophysics, University of California, Irvine, California 92697, USA.
University of California, Irvine · USHoward Hughes Medical Institute · USUniversity of Washington · US

Funding

Proteomics of the Proteasome Interacting NetworksR01GM074830 · NIGMS · UNIVERSITY OF CALIFORNIA-IRVINE · PI HUANG, LAN · 2005 to 2022
$6.1M
In Vivo Interactome and Dynamics of Cullin-Ring LigasesR01GM106003 · NIGMS · UNIVERSITY OF CALIFORNIA-IRVINE · PI HUANG, LAN, RYCHNOVSKY, SCOTT D. · 2013 to 2016
$772k
Howard Hughes Medical InstituteNIGMS NIH HHS R01 GM074830NIGMS NIH HHS R01GM074830NIGMS NIH HHS R01 GM106003NIGMS NIH HHS R01GM106003NIGMS NIH HHS T32-GM10856
6 · The paper itself

Abstract

The full enzymatic activity of the cullin-RING ubiquitin ligases (CRLs) requires a ubiquitin-like protein (that is, Nedd8) modification. By deamidating Gln40 of Nedd8 to glutamate (Q40E), the bacterial cycle-inhibiting factor (Cif) family is able to inhibit CRL E3 activities, thereby interfering with cellular functions. Despite extensive structural studies on CRLs, the molecular mechanism by which Nedd8 Gln40 deamidation affects CRL functions remains unclear. We apply a new quantitative cross-linking mass spectrometry approach to characterize three different types of full-length human Cul1-Rbx1 complexes and uncover major Nedd8-induced structural rearrangements of the CRL1 catalytic core. More importantly, we find that those changes are not induced by Nedd8(Q40E) conjugation, indicating that the subtle change of a single Nedd8 amino acid is sufficient to revert the structure of the CRL catalytic core back to its unmodified form. Our results provide new insights into how neddylation regulates the conformation and activity of CRLs.

Indexed as

Amino Acid MotifsCarrier ProteinsCatalytic DomainCullin ProteinsDeaminationGlutamic AcidGlutamineHumansMass SpectrometryNEDD8 ProteinProtein BindingSKP Cullin F-Box Protein LigasesUbiquitin-Protein LigasesUbiquitinsCarrier ProteinsCullin 1Cullin ProteinsCULL-RING ligase, humanGlutamic AcidGlutamineNEDD8 ProteinNEDD8 protein, humanRBX1 protein, humanSKP Cullin F-Box Protein LigasesUbiquitin-Protein LigasesUbiquitins

Identifiers

PMID26632597
PMCPMC4686759
OpenAlexW2189925267

What OpenQuestion holds

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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.