Evidence map›Paper›PMID 22190740›Full record

ArticleMolecular biology of the cell2012

Endoplasmic reticulum stress regulation of the Kar2p/BiP chaperone alleviates proteotoxicity via dual degradation pathways.

Chia-Ling Hsu, Rupali Prasad, Christie Blackman, Davis T W Ng

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
0.3field-weighted citation impact, top 44% 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

14 citing papers in PubMed, 20 citations in OpenAlex.

  1. Functional Characterization ofInternational journal of molecular sciences · 2026
    Article
  2. EngineeringEngineering microbiology · 2024
    Review
  3. Review
  4. The Transcriptome Response to Azole Compounds inJournal of fungi (Basel, Switzerland) · 2023
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. 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

4 authors at 2 institutions in 2 countries.

Chia-Ling HsuTemasek Life Sciences Laboratory, National University of Singapore, Singapore 117604.
Rupali Prasad
Christie Blackman
Davis T W Ng
Pennsylvania State University · USTemasek Life Sciences Laboratory · SG

Funding

CELLULAR TOLERANCE MECHANISM OF ABERRANT PROTEINSR01GM059171 · NIGMS · PENNSYLVANIA STATE UNIVERSITY-UNIV PARK · PI NG, DAVIS T.W. · 1999 to 2004
$1.1M
NIGMS NIH HHS GM059171NIGMS NIH HHS R01 GM059171
6 · The paper itself

Abstract

The unfolded protein response (UPR) monitors and maintains protein homeostasis in the endoplasmic reticulum (ER). In budding yeast, the UPR is a transcriptional regulatory pathway that is quiescent under normal conditions. Under conditions of acute ER stress, activation of UPR targets is essential for cell viability. How individual target genes contribute to stress tolerance is unclear. Uncovering these roles is hampered because most targets also play important functions in the absence of stress. To differentiate stress-specific roles from everyday functions, a single target gene was uncoupled from UPR control by eliminating its UPR-specific regulatory element. Through this approach, the UPR remains intact, aside from its inability to induce the designated target. Applying the strategy to the major ER chaperone Kar2p/BiP revealed the physiological function of increasing its cellular concentration. Despite hundreds of target genes under UPR control, we show that activation of KAR2 is indispensable to alleviate some forms of ER stress. Specifically, activation is essential to dispose misfolded proteins that are otherwise toxic. Surprisingly, induced BiP/Kar2p molecules are dedicated to alleviating stress. The inability to induce KAR2 under stress had no effect on its known housekeeping functions.

Indexed as

Unfolded Protein ResponseEndoplasmic Reticulum StressFungal ProteinsHSP70 Heat-Shock ProteinsMolecular ChaperonesProteolysisSaccharomyces cerevisiaeFungal ProteinsHSP70 Heat-Shock ProteinsKAR2 protein, yeastMolecular Chaperones

Identifiers

PMID22190740
PMCPMC3279391
OpenAlexW2009653694

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.