Evidence map›Paper›PMID 22199355›Full record

ArticleThe Journal of biological chemistry2012

Cdc37/Hsp90 protein-mediated regulation of IRE1α protein activity in endoplasmic reticulum stress response and insulin synthesis in INS-1 cells.

Asuka Ota, Yibin Wang

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
0.7field-weighted citation impact, top 32% 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

16 citing papers in PubMed, 39 citations in OpenAlex.

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  12. How Hsp90 and Cdc37 Lubricate Kinase Molecular Switches.Trends in biochemical sciences · 2017
    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

2 authors at 1 institution in 1 country.

Asuka OtaDivision of Molecular Medicine, Department of Anesthesiology, David Geffen School of Medicine, University of California, Los Angeles, California 90095, USA.
Yibin Wang
University of California, Los Angeles · US

Funding

Novel mechanisms in ER regulation in heartR01HL070079 · NHLBI · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI WANG, YIBIN · 2003 to 2011
$3.2M
A Novel Mechanism in p38 Stress Kinase RegulationF31AG032163 · NIA · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI OTA, ASUKA · 2008 to 2009
$44k
NHLBI NIH HHS HL070079NHLBI NIH HHS R01 HL070079NIA NIH HHS F31 AG032163NIA NIH HHS F31AG032163PHS HHS 088640
6 · The paper itself

Abstract

IRE1α is an endoplasmic reticulum (ER) localized signaling molecule critical for unfolded protein response. During ER stress, IRE1α activation is induced by oligomerization and autophosphorylation in its cytosolic domain, a process triggered by dissociation of an ER luminal chaperone, binding immunoglobulin-protein (BiP), from IRE1α. In addition, inhibition of a cytosolic chaperone protein Hsp90 also induces IRE1α oligomerization and activation in the absence of an ER stressor. Here, we report that the Hsp90 cochaperone Cdc37 directly interacts with IRE1α through a highly conserved cytosolic motif of IRE1α. Cdc37 knockdown or disruption of Cdc37 interaction with IRE1α significantly increased basal IRE1α activity. In INS-1 cells, Hsp90 inhibition and disruption of IRE1α-Cdc37 interaction both induced an ER stress response and impaired insulin synthesis and secretion. These data suggest that Cdc37-mediated direct interaction between Hsp90/Cdc37 and an IRE1α cytosolic motif is important to maintain basal IRE1α activity and contributes to normal protein homeostasis and unfolded protein response under physiological stimulation.

Indexed as

Amino Acid SequenceCell Cycle ProteinsCells, CulturedChaperoninsCytosolDimerizationEndoplasmic Reticulum StressEndoribonucleasesGlucoseHeLa CellsHSP90 Heat-Shock ProteinsHumansInsulinInsulin-Secreting CellsInsulin SecretionMolecular Sequence DataCDC37 protein, humanCell Cycle ProteinsChaperoninsEndoribonucleasesERN1 protein, humanGlucoseHSP90 Heat-Shock ProteinsInsulinProtein Serine-Threonine Kinases

Identifiers

PMID22199355
PMCPMC3307264
OpenAlexW2081677105

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.