Evidence map›Paper›PMID 15371354›Full record

ArticleGenetics2004

Role of the unfolded protein response pathway in secretory stress and regulation of INO1 expression in Saccharomyces cerevisiae.

Hak J Chang, Stephen A Jesch, Maria L Gaspar, Susan A Henry

Open access · bronzeAbstract read
In one paragraph

Article in Genetics, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
1.7field-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

42 citing papers in PubMed, 74 citations in OpenAlex.

  1. Article
  2. Architecture and function of yeast phosphatidate phosphatase Pah1 domains/regions.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2024
    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

4 authors at 2 institutions in 1 country.

Hak J ChangDepartment of Biological Sciences, Carnegie Mellon University, Pittsburgh, Pennsylvania 15213, USA.
Stephen A Jesch
Maria L Gaspar
Susan A Henry
Cornell University · USCarnegie Mellon University · US

Funding

GENETICS AND DEVELOPMENT OF YEAST MEMBRANE MUTANTSR01GM019629 · NIGMS · YESHIVA UNIVERSITY · PI HENRY, SUSAN ARMSTRONG · 1985 to 2015
$6.0M
GENETIC REGULATION OF PHOSPHOLIPID SYNTHESIS IN YEASTR37GM019629 · NIGMS · CORNELL UNIVERSITY ITHACA · PI HENRY, SUSAN A. · 1991 to 2000
$426k
STRUCTURE/FUNCTION ANALYSIS OF PHA4 IN C ELEGANSF32GM019629 · NIGMS · UNIVERSITY OF UTAH · PI KALTENBACH, LINDA S · 1999 to 2001
$59k
NIGMS NIH HHS F32 GM019629NIGMS NIH HHS GM-19629NIGMS NIH HHS R01 GM019629NIGMS NIH HHS R37 GM019629
6 · The paper itself

Abstract

The unfolded protein response pathway (UPR) enables the cell to cope with the buildup of unfolded proteins in the endoplasmic reticulum (ER). UPR loss-of-function mutants, hac1Delta and ire1Delta, are also inositol auxotrophs, a phenotype associated with defects in expression of INO1, the most highly regulated of a set of genes encoding enzymes of phospholipid metabolism. We now demonstrate that the UPR plays a functional role in membrane trafficking under conditions of secretory stress in yeast. Mutations conferring a wide range of membrane trafficking defects exhibited negative genetic interaction when combined with ire1Delta and hac1Delta. At semipermissive temperatures, carboxypeptidase Y transit time to the vacuole was slower in Sec(-) cells containing an ire1Delta or hac1Delta mutation than in Sec(-) cells with an intact UPR. The UPR was induced in Sec(-) cells defective in subcellular membrane trafficking events ranging from ER vesicle trafficking to distal secretion and in erg6Delta cells challenged with brefeldin A. However, the high levels of UPR induction observed under these conditions were not correlated with elevated INO1 expression. Indeed, many of the Sec(-) mutants that had elevated UPR expression at semipermissive growth temperatures failed to achieve wild-type levels of INO1 expression under these same conditions.

Indexed as

Basic-Leucine Zipper Transcription FactorsCell MembraneGene Expression RegulationKineticsLipid MetabolismMembrane GlycoproteinsMutationMyo-Inositol-1-Phosphate SynthaseProtein Serine-Threonine KinasesProtein TransportRepressor ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTime FactorsTranscription FactorsVacuolesBasic-Leucine Zipper Transcription FactorsHAC1 protein, S cerevisiaeIRE1 protein, S cerevisiaeMembrane GlycoproteinsMyo-Inositol-1-Phosphate SynthaseProtein Serine-Threonine KinasesRepressor ProteinsSaccharomyces cerevisiae ProteinsTranscription Factors

Identifiers

PMID15371354
PMCPMC1448725
OpenAlexW2154094694

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.