Evidence map›Paper›PMID 29061306›Full record

ArticleBiochemical and biophysical research communications2017

SUMOylation represses the transcriptional activity of the Unfolded Protein Response transducer ATF6.

Xia Hou, Zhao Yang, Kezhong Zhang, Deyu Fang, Fei Sun

Abstract read
In one paragraph

Article in Biochemical and biophysical research communications, 2017. 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
0.6field-weighted citation impact, top 33% 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, 14 citations in OpenAlex.

  1. Article
  2. Review
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  5. Article
  6. Review
  7. Function and regulation of ubiquitin-like SUMO system in heart.Frontiers in cell and developmental biology · 2023
    Review
  8. Review
  9. Review
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  11. Review
  12. Review
  13. Article
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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

5 authors at 3 institutions in 2 countries.

Xia HouDepartment of Physiology, Wayne State University School of Medicine, Detroit, MI 48201, USA; Department of Biochemistry and Molecular Biology, Jiamusi University School of Basic Medicine, Jiamusi, Heilongjiang, 154007, China.
Zhao YangCenter for Molecular Medicine and Genetics, Wayne State University School of Medicine, Detroit, MI 48201, USA.
Kezhong ZhangCenter for Molecular Medicine and Genetics, Wayne State University School of Medicine, Detroit, MI 48201, USA; Department of Microbiology, Immunology and Biochemistry, Wayne State University School of Medicine, Detroit, MI 48201, USA. Electronic address: kzhang@med.wayne.edu.
Deyu FangDepartment of Pathology, Northwestern University Feinberg School of Medicine, Chicago, IL 60611, USA. Electronic address: fangd@northwestern.edu.
Fei SunDepartment of Physiology, Wayne State University School of Medicine, Detroit, MI 48201, USA. Electronic address: fsun@med.wayne.edu.
Wayne State University · USJiamusi University · CNNorthwestern University · US

Funding

Regulation of Hepatic Steatosis by an ER Stress-Inducible Transcription Factor CRR01DK090313 · NIDDK · WAYNE STATE UNIVERSITY · PI Kezhong Zhang · 2011 to 2026
$5.0M
The roles of Sirt1, a deacetylase, in immune tolerance and autoimmunityR01AI079056 · NIAID · UNIVERSITY OF MISSOURI-COLUMBIA · PI FANG, DEYU · 2008 to 2017
$3.3M
Rabbit model for cystic fibrosisR01HL133162 · NHLBI · WAYNE STATE UNIVERSITY · PI JIN, JIAN-PING, XU, JIE · 2016 to 2019
$2.9M
Simultaneous Targeting of IRE1a in B Cells and Macrophages for Lupus TherapyR01AR066634 · NIAMS · NORTHWESTERN UNIVERSITY AT CHICAGO · PI FANG, DEYU, ZHANG, KEZHONG · 2014 to 2018
$1.7M
Airborne Particulate Matter, Endoplasmic Reticulum Stress and Hepatic Lipid DysreR21ES017829 · NIEHS · WAYNE STATE UNIVERSITY · PI ZHANG, KEZHONG · 2010 to 2011
$442k
NHLBI NIH HHS R01 HL133162NIAID NIH HHS R01 AI079056NIAMS NIH HHS R01 AR066634NIDDK NIH HHS R01 DK090313NIEHS NIH HHS R21 ES017829
6 · The paper itself

Abstract

The Unfolded Protein Response (UPR) is a cascade of intracellular stress signaling from the endoplasmic reticulum (ER) that protect the cells from the stress caused by accumulation of unfolded or misfolded proteins in the ER. Activating transcription factor 6 (ATF6) is one of primary UPR transducers that remodels the stressed cells through transcriptional regulation. Although the activation mechanism and biological roles of ATF6 have been well studied, the understanding of the negative or feedback regulation of ATF6 remains elusive. In this report, we showed that ATF6 protein can be modified by small ubiquitin-like modification (SUMOylation) and that the transcriptional activity of ATF6 is negatively regulated by SUMOylation. We identified that SUMOylation of ATF6 is significantly increased in the cells expressing misfolded cystic fibrosis transmembrane conductance regulator (CFTR) encoded by the mutant human CFTR gene (dF508CFTR). Further analyses revealed two highly conserved SUMOylation motifs within the trans-activation domain of ATF6 protein of human, mouse, or rat specie. The human ATF6 protein can be SUMOylated mediated through the small ubiquitin-like modifier protein 1 (SUMO-1) and E3 SUMO-protein ligase 1 (PIAS1) at the conserved sumoylation residue Lys

Indexed as

Activating Transcription Factor 6Endoplasmic Reticulum StressFeedback, PhysiologicalRepressor ProteinsSUMO-1 ProteinSumoylationTranscriptional ActivationUnfolded Protein ResponseActivating Transcription Factor 6ATF6 protein, humanRepressor ProteinsSUMO-1 ProteinATF6CFTRER stressSUMOylationTranscriptionUPR

Identifiers

PMID29061306
PMCPMC5698096
OpenAlexW2766237980

What OpenQuestion holds

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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.