Evidence map›Paper›PMID 19748355›Full record

ArticleMolecular cell2009

F-box-directed CRL complex assembly and regulation by the CSN and CAND1.

Michael W Schmidt, Philip R McQuary, Susan Wee, Kay Hofmann, Dieter A Wolf

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 69 papers.

0numbers the graph read from it
0cells of the map it votes in
69citing papers in PubMed
5.4field-weighted citation impact, top 3% 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

69 citing papers in PubMed, 122 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Quantitative analyses for effects of neddylation on CRL2Protein science : a publication of the Protein Society · 2021
    Article
  10. Review
  11. Article
  12. Review
  13. Review
  14. Article
  15. Article
  16. CRL4The EMBO journal · 2018
    Article
  17. Article
  18. Article
  19. Article
  20. Article

9 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 3 institutions in 2 countries.

Michael W SchmidtDepartment of Genetics and Complex Diseases, Harvard School of Public Health, Boston, MA 02115, USA.
Philip R McQuary
Susan Wee
Kay Hofmann
Dieter A Wolf
Harvard University · USMiltenyi Biotec (Germany) · DESanford Burnham Prebys Medical Discovery Institute · US

Funding

Global Approaches to Protein UbiquitylationR01GM059780 · NIGMS · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI WOLF, DIETER A · 1999 to 2010
$3.8M
NIGMS NIH HHS GM59780NIGMS NIH HHS R01 GM059780
6 · The paper itself

Abstract

The COP9 signalosome (CSN) is thought to maintain the stability of cullin-RING ubiquitin ligases (CRL) by limiting the autocatalytic destruction of substrate adapters such as F box proteins (FBPs). CAND1, a protein associated with unneddylated CUL1, was proposed to assist in this role in an as yet unclear fashion. We found that only a subset of Schizosaccharomyces pombe FBPs, which feature a critical F box proline that promotes their interaction with CUL1, required CSN for stability. Unlike the CRL3 adaptor Btb3p, none of the CSN-sensitive FBPs were affected by deletion of ubp12. Contrary to current models, CAND1 does not control adaptor stability but maintains the cellular balance of CRL1 complexes by preventing rare FBPs from being outcompeted for binding to CUL1 by more ample adapters. These findings were integrated into a refined model of CRL control in which substrate availability toggles CRLs between independent CSN and CAND1 cycles.

Indexed as

Amino Acid SequenceCDC2 Protein KinaseConserved SequenceCOP9 Signalosome ComplexCullin ProteinsEndopeptidasesF-Box ProteinsMetalloproteasesModels, MolecularMolecular Sequence DataMultiprotein ComplexesMutationPeptide HydrolasesProlineProtein BindingProtein StabilityCDC2 Protein Kinasecdc2 protein, S pombeCOP9 Signalosome ComplexCsn5 protein, S pombeCullin ProteinsEndopeptidasesF-Box ProteinsMetalloproteasesMultiprotein ComplexesNed8 protein, S pombePeptide HydrolasesPof10 protein, S pombePof3 protein, S pombeProlineSchizosaccharomyces pombe ProteinsSKP1 protein, S pombeSKP Cullin F-Box Protein LigasesUbiquitinsUbp12 protein, S pombe

Identifiers

PMID19748355
PMCPMC2779159
OpenAlexW2032820757

What OpenQuestion holds

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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.