Evidence map›Paper›PMID 21926971›Full record

ArticleThe EMBO journal2011

BAX inhibitor-1 regulates autophagy by controlling the IRE1α branch of the unfolded protein response.

Karen Castillo, Diego Rojas-Rivera, Fernanda Lisbona, Benjamín Caballero, Melissa Nassif, Felipe A Court, Sebastian Schuck, Consuelo Ibar, Peter Walter, Jimena Sierralta and 2 more

Erratum issuedOpen access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 67 papers, 3 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
67citing papers in PubMed, 3 pooled it
7.0field-weighted citation impact, top 3% 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

67 citing papers in PubMed, 3 syntheses or guidelines pooled it, 111 citations in OpenAlex.

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  15. Regulation of lipid metabolism by the unfolded protein response.Journal of cellular and molecular medicine · 2021
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7 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

12 authors at 5 institutions in 3 countries.

Karen CastilloCenter for Molecular Studies of the Cell, Department of Cellular and Molecular Biology, Institute of Biomedical Sciences, University of Chile, Santiago, Chile.
Diego Rojas-Rivera
Fernanda Lisbona
Benjamín Caballero
Melissa Nassif
Felipe A Court
Sebastian Schuck
Consuelo Ibar
Peter Walter
Jimena Sierralta
Alvaro Glavic
Claudio Hetz
Instituto de Neurociencia Biomédica · CLUniversity of Chile · CLHoward Hughes Medical Institute · USHarvard University · USMillennium Science Initiative · CL

Funding

Howard Hughes Medical Institute
6 · The paper itself

Abstract

Both autophagy and apoptosis are tightly regulated processes playing a central role in tissue homeostasis. Bax inhibitor 1 (BI-1) is a highly conserved protein with a dual role in apoptosis and endoplasmic reticulum (ER) stress signalling through the regulation of the ER stress sensor inositol requiring kinase 1 α (IRE1α). Here, we describe a novel function of BI-1 in the modulation of autophagy. BI-1-deficient cells presented a faster and stronger induction of autophagy, increasing LC3 flux and autophagosome formation. These effects were associated with enhanced cell survival under nutrient deprivation. Repression of autophagy by BI-1 was dependent on cJun-N terminal kinase (JNK) and IRE1α expression, possibly due to a displacement of TNF-receptor associated factor-2 (TRAF2) from IRE1α. Targeting BI-1 expression in flies altered autophagy fluxes and salivary gland degradation. BI-1 deficiency increased flies survival under fasting conditions. Increased expression of autophagy indicators was observed in the liver and kidney of bi-1-deficient mice. In summary, we identify a novel function of BI-1 in multicellular organisms, and suggest a critical role of BI-1 as a stress integrator that modulates autophagy levels and other interconnected homeostatic processes.

Indexed as

AcidsAnimalsAutophagyCells, CulturedCell SurvivalDrosophilaEndoribonucleasesMembrane ProteinsMiceOrganisms, Genetically ModifiedPhagosomesProtein Serine-Threonine KinasesSaccharomyces cerevisiaeSignal TransductionStarvationTransport VesiclesAcidsEndoribonucleasesErn1 protein, mouseMembrane ProteinsProtein Serine-Threonine KinasesTmbim6 protein, mouse

Identifiers

PMID21926971
PMCPMC3230375
OpenAlexW1797345114

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.