Evidence map›Paper›PMID 19520858›Full record

ArticleThe Journal of biological chemistry2009

Degradation of sterol regulatory element-binding protein precursor requires the endoplasmic reticulum-associated degradation components Ubc7 and Hrd1 in fission yeast.

Bridget T Hughes, Christine C Nwosu, Peter J Espenshade

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
1.5field-weighted citation impact, top 20% 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

23 citing papers in PubMed, 34 citations in OpenAlex.

  1. Article
  2. Exogenous HJournal of cachexia, sarcopenia and muscle · 2023
    Article
  3. Article
  4. Outline of the biosynthesis and regulation of ergosterol in yeast.World journal of microbiology & biotechnology · 2019
    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

3 authors at 1 institution in 1 country.

Bridget T HughesDepartment of Cell Biology, The Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA.
Christine C Nwosu
Peter J Espenshade
Johns Hopkins University · US

Funding

Regulation of Cellular Cholesterol HomeostasisR01HL077588 · NHLBI · JOHNS HOPKINS UNIVERSITY · PI ESPENSHADE, PETER J. · 2004 to 2022
$7.8M
NHLBI NIH HHS HL-077588NHLBI NIH HHS R01 HL077588
6 · The paper itself

Abstract

Sre1, the fission yeast sterol regulatory element-binding protein (SREBP), is an endoplasmic reticulum (ER) membrane-bound transcription factor that is a principal regulator of hypoxic gene expression. Under low oxygen, Sre1 is cleaved from its inactive ER precursor form to generate an active nuclear transcription factor that up-regulates genes required for low oxygen growth. To maintain a constant supply of Sre1, Sre1 precursor synthesis must be regulated to replenish Sre1 precursor lost to proteolytic cleavage under low oxygen. In this study, we investigated the mechanisms controlling Sre1 precursor levels. We found that positive feedback regulation at the sre1(+) promoter increases the synthesis of the Sre1 precursor under low oxygen and that this regulation is required for maximal Sre1 activation and target gene expression. We also demonstrate that the Sre1 precursor is rapidly degraded by the proteasome in the absence of its binding partner Scp1, which is required for oxygen-regulated Sre1 cleavage. Degradation of Sre1 in the absence of Scp1 requires the ER-associated degradation (ERAD) components Ubc7, an E2 ubiquitin conjugating enzyme, and Hrd1, an E3 ubiquitin ligase. We conclude that positive feedback regulation to up-regulate Sre1 precursor synthesis under low oxygen is essential for Sre1 function and propose that excess Sre1 precursor is removed by ERAD to ensure complex formation between Sre1 and its binding partner Scp1. Thus, Sre1 is a new example of an endogenous ERAD substrate, establishing fission yeast as an organism for the study of this important degradative pathway.

Indexed as

Protein Processing, Post-TranslationalEndoplasmic ReticulumFeedback, PhysiologicalMicrofilament ProteinsPromoter Regions, GeneticProteasome Endopeptidase ComplexProtein PrecursorsProtein StabilitySchizosaccharomycesSchizosaccharomyces pombe ProteinsSterol Regulatory Element Binding ProteinsUbiquitin-Conjugating EnzymesUbiquitin-Protein LigasesHrd1 protein, S pombeMicrofilament ProteinsProteasome Endopeptidase ComplexProtein PrecursorsSchizosaccharomyces pombe ProteinsScp1 protein, S pombeSre1 protein, S pombeSterol Regulatory Element Binding ProteinsUbc7 protein, S pombeUbiquitin-Conjugating EnzymesUbiquitin-Protein Ligases

Identifiers

PMID19520858
PMCPMC2742815
OpenAlexW2052900902

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.