Evidence map›Paper›PMID 21172660›Full record

ArticleMolecular cell2010

A transcriptional activator is part of an SCF ubiquitin ligase to control degradation of its cofactors.

Ikram Ouni, Karin Flick, Peter Kaiser

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
1.6field-weighted citation impact, top 18% 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, 47 citations in OpenAlex.

  1. Article
  2. Distinct Stress Regulators in the CRL Family: Emerging Roles of F-Box Proteins: Cullin-RING Ligases and Stress-Sensing.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025
    Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Transcription Factor Condensates Mediate Clustering ofbioRxiv : the preprint server for biology · 2024
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Review
  14. Cdc48 cofactor Shp1 regulates signal-induced SCFProceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

Ikram OuniDepartment of Biological Chemistry, School of Medicine, University of California, Irvine, 240D Med Sci I, Irvine, CA 92697-1700, USA.
Karin Flick
Peter Kaiser
University of California, Irvine · US

Funding

Ubiquitin SignalingR01GM066164 · NIGMS · UNIVERSITY OF CALIFORNIA-IRVINE · PI KAISER, PETER · 2002 to 2022
$7.4M
Translational Research in Cancer Genomic MedicineT32CA113265 · NCI · UNIVERSITY OF CALIFORNIA-IRVINE · PI LEE, WEN-HWA · 2007 to 2011
$1.4M
Regulation by Proteolysis-Independent UbiquitinationR56GM066164 · NIGMS · UNIVERSITY OF CALIFORNIA-IRVINE · PI KAISER, PETER · 2007 to 2007
$265k
Autism Speaks GM66164AS1NCI NIH HHS T32 CA113265NIGMS NIH HHS GM66164NIGMS NIH HHS R01 GM066164NIGMS NIH HHS R56 GM066164
6 · The paper itself

Abstract

Multisubunit protein complexes pose a challenge to the coordinated regulation of individual components. We show how the yeast transactivating factor Met4 functions as a component of the SCF(Met30) ubiquitin ligase to synchronize its own activity with cofactor assembly. Cells maintain Met4 in a dormant state by a regulatory ubiquitin chain assembled by SCF(Met30). Nutritional and heavy-metal stress block Met4 ubiquitylation resulting in Met4 activation, which induces a stress-response program including cell-cycle arrest. Met4 relies on assembly with various cofactors for promoter binding. We report here that the stability of these DNA-binding cofactors is regulated by SCF(Met30). Remarkably, the transcriptional activator Met4 functions as a substrate-specificity factor in the context of SCF(Met30/Met4) to coordinate cofactor degradation with its own activity status. Our results establish an additional layer for substrate recruitment by SCF ubiquitin ligases and provide conceptual insight into coordinated regulation of protein complexes.

Indexed as

Basic-Leucine Zipper Transcription FactorsDNA-Binding ProteinsF-Box ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsUbiquitin-Protein Ligase ComplexesBasic-Leucine Zipper Transcription FactorsDNA-Binding ProteinsF-Box ProteinsMET30 protein, S cerevisiaeMET4 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsUbiquitin-Protein Ligase Complexes

Identifiers

PMID21172660
PMCPMC3026289
OpenAlexW2021913420

What OpenQuestion holds

Textmetadata
LicenceTDM
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.