Evidence map›Paper›PMID 17108329›Full record

ArticleMolecular biology of the cell2007

SCFCdc4-mediated degradation of the Hac1p transcription factor regulates the unfolded protein response in Saccharomyces cerevisiae.

Bhupinder Pal, Nickie C Chan, Leon Helfenbaum, Kaeling Tan, William P Tansey, Mary-Jane Gething

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.0field-weighted citation impact, top 26% 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

21 citing papers in PubMed, 35 citations in OpenAlex.

  1. Article
  2. Article
  3. DoesMicroorganisms · 2021
    Article
  4. Article
  5. Review
  6. Translation Control ofInternational journal of molecular sciences · 2019
    Review
  7. Article
  8. Article
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  11. Review
  12. Article
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  18. Review
  19. Article
  20. Rationalizing translation attenuation in the network architecture of the unfolded protein response.Proceedings of the National Academy of Sciences of the United States of America · 2008
    Article
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

6 authors at 2 institutions in 2 countries.

Bhupinder PalDepartment of Biochemistry and Molecular Biology, University of Melbourne, Victoria 3010, Australia.
Nickie C Chan
Leon Helfenbaum
Kaeling Tan
William P Tansey
Mary-Jane Gething
The University of Melbourne · AUCold Spring Harbor Laboratory · US

Funding

Transcription Control By The Ubiquitin-Proteasome SystemR01GM067728 · NIGMS · VANDERBILT UNIVERSITY · PI TANSEY, WILLIAM PATRICK · 2003 to 2015
$4.6M
NIGMS NIH HHS GM-067728NIGMS NIH HHS R01 GM067728
6 · The paper itself

Abstract

The Saccharomyces cerevisiae basic leucine zipper transcription factor Hac1p is synthesized in response to the accumulation of unfolded polypeptides in the lumen of the endoplasmic reticulum (ER), and it is responsible for up-regulation of approximately 5% of all yeast genes, including ER-resident chaperones and protein-folding catalysts. Hac1p is one of the most short-lived yeast proteins, having a half-life of approximately 1.5 min. Here, we have shown that Hac1p harbors a functional PEST degron and that degradation of Hac1p by the proteasome involves the E2 ubiquitin-conjugating enzyme Ubc3/Cdc34p and the SCF(Cdc4) E3 complex. Consistent with the known nuclear localization of Cdc4p, rapid degradation of Hac1p requires the presence of a functional nuclear localization sequence, which we demonstrated to involve basic residues in the sequence (29)RKRAKTK(35). Two-hybrid analysis demonstrated that the PEST-dependent interaction of Hac1p with Cdc4p requires Ser146 and Ser149. Turnover of Hac1p may be dependent on transcription because it is inhibited in cell mutants lacking Srb10 kinase, a component of the SRB/mediator module of the RNA polymerase II holoenzyme. Stabilization of Hac1p by point mutation or deletion, or as the consequence of defects in components of the degradation pathway, results in increased unfolded protein response element-dependent transcription and improved cell viability under ER stress conditions.

Indexed as

Amino Acid MotifsAmino Acid SequenceAnaphase-Promoting Complex-CyclosomeBasic-Leucine Zipper Transcription FactorsBinding SitesCell Cycle ProteinsCell NucleusCell SurvivalCyclin-Dependent Kinase 8Cyclin-Dependent KinasesF-Box ProteinsMitogen-Activated Protein Kinase KinasesMolecular Sequence DataMutationProteasome Endopeptidase ComplexProtein FoldingAnaphase-Promoting Complex-CyclosomeBasic-Leucine Zipper Transcription FactorsCDC34 protein, S cerevisiaeCDC4 protein, S cerevisiaeCell Cycle ProteinsCyclin-Dependent Kinase 8Cyclin-Dependent KinasesF-Box ProteinsHAC1 protein, S cerevisiaeMitogen-Activated Protein Kinase KinasesProteasome Endopeptidase ComplexRepressor ProteinsSaccharomyces cerevisiae ProteinsSerineSSN3 protein, S cerevisiaeTranscription FactorsUbiquitinUbiquitin-Conjugating EnzymesUbiquitin-Protein Ligase ComplexesUbiquitin-Protein Ligases

Identifiers

PMID17108329
PMCPMC1783797
OpenAlexW2098109141

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.