Evidence map›Paper›PMID 26966233›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2016

Unfolded protein response regulates yeast small GTPase Arl1p activation at late Golgi via phosphorylation of Arf GEF Syt1p.

Jia-Wei Hsu, Pei-Hua Tang, I-Hao Wang, Chia-Lun Liu, Wen-Hui Chen, Pei-Chin Tsai, Kuan-Yu Chen, Kuan-Jung Chen, Chia-Jung Yu, Fang-Jen S Lee

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.1field-weighted citation impact, top 24% 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

11 citing papers in PubMed, 17 citations in OpenAlex.

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  6. Tunicamycin Protects against LPS-Induced Lung Injury.Pharmaceuticals (Basel, Switzerland) · 2022
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  10. 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

10 authors at 2 institutions in 1 country.

Jia-Wei HsuInstitute of Molecular Medicine, College of Medicine, National Taiwan University, Taipei 100, Taiwan; Department of Medical Research, National Taiwan University Hospital, Taipei 100, Taiwan;
Pei-Hua TangInstitute of Molecular Medicine, College of Medicine, National Taiwan University, Taipei 100, Taiwan; Department of Medical Research, National Taiwan University Hospital, Taipei 100, Taiwan;
I-Hao WangInstitute of Molecular Medicine, College of Medicine, National Taiwan University, Taipei 100, Taiwan; Department of Medical Research, National Taiwan University Hospital, Taipei 100, Taiwan;
Chia-Lun LiuInstitute of Molecular Medicine, College of Medicine, National Taiwan University, Taipei 100, Taiwan; Department of Medical Research, National Taiwan University Hospital, Taipei 100, Taiwan;
Wen-Hui ChenInstitute of Molecular Medicine, College of Medicine, National Taiwan University, Taipei 100, Taiwan; Department of Medical Research, National Taiwan University Hospital, Taipei 100, Taiwan;
Pei-Chin TsaiInstitute of Molecular Medicine, College of Medicine, National Taiwan University, Taipei 100, Taiwan; Department of Medical Research, National Taiwan University Hospital, Taipei 100, Taiwan;
Kuan-Yu ChenInstitute of Molecular Medicine, College of Medicine, National Taiwan University, Taipei 100, Taiwan; Department of Medical Research, National Taiwan University Hospital, Taipei 100, Taiwan;
Kuan-Jung ChenInstitute of Molecular Medicine, College of Medicine, National Taiwan University, Taipei 100, Taiwan; Department of Medical Research, National Taiwan University Hospital, Taipei 100, Taiwan;
Chia-Jung YuDepartment of Cell and Molecular Biology, College of Medicine, Chang Gung University, Tao-Yuan 333, Taiwan.
Fang-Jen S LeeInstitute of Molecular Medicine, College of Medicine, National Taiwan University, Taipei 100, Taiwan; Department of Medical Research, National Taiwan University Hospital, Taipei 100, Taiwan; fangjen@ntu.edu.tw.ORCID http://orcid.org/0000-0002-2167-2426
National Taiwan University · TWChang Gung University · TW

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

ADP ribosylation factor (Arf) GTPases are key regulators of membrane traffic at the Golgi complex. In yeast, Arf guanine nucleotide-exchange factor (GEF) Syt1p activates Arf-like protein Arl1p, which was accompanied by accumulation of golgin Imh1p at late Golgi, but whether and how this function of Syt1p is regulated remains unclear. Here, we report that the inositol-requiring kinase 1 (Ire1p)-mediated unfolded protein response (UPR) modulated Arl1p activation at late Golgi. Arl1p activation was dependent on both kinase and endo-RNase activities of Ire1p. Moreover, constitutively active transcription factor Hac1p restored the Golgi localization of Arl1p and Imh1p inIRE1-deleted cells. Elucidating the mechanism of Ire1p-Hac1p axis actions, we found that it regulated phosphorylation of Syt1p, which enhances Arl1p activation, recruitment of Imh1p to the Golgi, and Syt1p interaction with Arl1p. Consistent with these findings, the induction of UPR by tunicamycin treatment increases phosphorylation of Syt1p, resulting in Arl1p activation. Thus, these findings clarify how the UPR influences the roles of Syt1p, Arl1p, and Imh1p in Golgi transport.

Indexed as

Protein Processing, Post-TranslationalBasic-Leucine Zipper Transcription FactorsEndoplasmic Reticulum StressGenes, ReporterGolgi ApparatusGuanine Nucleotide Exchange FactorsMembrane GlycoproteinsMonomeric GTP-Binding ProteinsPhosphorylationProtein Serine-Threonine KinasesProtein TransportRecombinant Fusion ProteinsRepressor ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsUnfolded Protein ResponseARL1 protein, S cerevisiaeBasic-Leucine Zipper Transcription FactorsGuanine Nucleotide Exchange FactorsHAC1 protein, S cerevisiaeIMH1 protein, S cerevisiaeIRE1 protein, S cerevisiaeMembrane GlycoproteinsMonomeric GTP-Binding ProteinsProtein Serine-Threonine KinasesRecombinant Fusion ProteinsRepressor ProteinsSaccharomyces cerevisiae ProteinsSYT1 protein, S cerevisiaeVesicular Transport ProteinsADP ribosylation factorER stressGolgi complexGTPaseUPR

Identifiers

PMID26966233
PMCPMC4812715
OpenAlexW2295622577

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.