Evidence map›Paper›PMID 27920251›Full record

ArticleMolecular and cellular biology2017

A Homeostatic Shift Facilitates Endoplasmic Reticulum Proteostasis through Transcriptional Integration of Proteostatic Stress Response Pathways.

Liam Baird, Tadayuki Tsujita, Eri H Kobayashi, Ryo Funayama, Takeshi Nagashima, Keiko Nakayama, Masayuki Yamamoto

Open access · bronzeAbstract read
In one paragraph

Article in Molecular and cellular biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
3.2field-weighted citation impact, top 9% 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

36 citing papers in PubMed, 59 citations in OpenAlex.

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  7. Unique and overlapping roles of NRF2 and NRF1 in transcriptional regulation.Journal of clinical biochemistry and nutrition · 2024
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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

7 authors at 3 institutions in 1 country.

Liam BairdDepartment of Medical Biochemistry, Tohoku University Graduate School of Medicine, Sendai, Japan liambaird@med.tohoku.ac.jp masiyamamoto@med.tohoku.ac.jp.
Tadayuki TsujitaLaboratory of Biochemistry, Department of Applied Biochemistry and Food Science, Faculty of Agriculture, Saga University, Saga, Japan.
Eri H KobayashiDepartment of Medical Biochemistry, Tohoku University Graduate School of Medicine, Sendai, Japan.
Ryo FunayamaDivision of Cell Proliferation, Tohoku University Graduate School of Medicine, Sendai, Japan.
Takeshi NagashimaDivision of Cell Proliferation, Tohoku University Graduate School of Medicine, Sendai, Japan.
Keiko NakayamaDivision of Cell Proliferation, Tohoku University Graduate School of Medicine, Sendai, Japan.
Masayuki YamamotoDepartment of Medical Biochemistry, Tohoku University Graduate School of Medicine, Sendai, Japan liambaird@med.tohoku.ac.jp masiyamamoto@med.tohoku.ac.jp.
Tohoku University · JPSaga University · JPTohoku Medical Megabank Organization · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Eukaryotic cells maintain protein homeostasis through the activity of multiple basal and inducible systems, which function in concert to allow cells to adapt to a wide range of environmental conditions. Although the transcriptional programs regulating individual pathways have been studied in detail, it is not known how the different pathways are transcriptionally integrated such that a deficiency in one pathway can be compensated by a change in an auxiliary response. One such pathway that plays an essential role in many proteostasis responses is the ubiquitin-proteasome system, which functions to degrade damaged, unfolded, or short half-life proteins. Transcriptional regulation of the proteasome is mediated by the transcription factor Nrf1. Using a conditional knockout mouse model, we found that Nrf1 regulates protein homeostasis in the endoplasmic reticulum (ER) through transcriptional regulation of the ER stress sensor ATF6. In Nrf1 conditional-knockout mice, a reduction in proteasome activity is accompanied by an ATF6-dependent downregulation of the endoplasmic reticulum-associated degradation machinery, which reduces the substrate burden on the proteasome. This indicates that Nrf1 regulates a homeostatic shift through which proteostasis in the endoplasmic reticulum and cytoplasm are coregulated based on a cell's ability to degrade proteins.

Indexed as

HomeostasisTranscription, GeneticActivating Transcription Factor 6AnimalsBinding SitesChromatin ImmunoprecipitationDown-RegulationEndoplasmic ReticulumEndoplasmic Reticulum-Associated DegradationEndoplasmic Reticulum StressEnhancer Elements, GeneticMaleMembrane ProteinsMice, KnockoutModels, BiologicalNuclear Respiratory Factor 1Activating Transcription Factor 6Ern2 protein, mouseMembrane ProteinsNrf1 protein, mouseNuclear Respiratory Factor 1Proteasome Endopeptidase ComplexProtein Serine-Threonine KinasesERADER stressNrf1proteasomeproteostasisUPR

Identifiers

PMID27920251
PMCPMC5288573
OpenAlexW2560228809

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.