Evidence map›Paper›PMID 31201345›Full record

ArticleScientific reports2019

Membrane phospholipid alteration causes chronic ER stress through early degradation of homeostatic ER-resident proteins.

Peter Shyu, Benjamin S H Ng, Nurulain Ho, Ruijie Chaw, Yi Ling Seah, Charlie Marvalim, Guillaume Thibault

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed
4.0field-weighted citation impact, top 6% 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

52 citing papers in PubMed, 83 citations in OpenAlex.

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  17. Lipids: Driving Forces in the Underlying Biology of Carcinogenesis.ACS pharmacology & translational science · 2025
    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

7 authors at 1 institution in 1 country.

Peter ShyuSchool of Biological Sciences, Nanyang Technological University, Singapore, 637551, Singapore.
Benjamin S H NgSchool of Biological Sciences, Nanyang Technological University, Singapore, 637551, Singapore.
Nurulain HoSchool of Biological Sciences, Nanyang Technological University, Singapore, 637551, Singapore.
Ruijie ChawSchool of Biological Sciences, Nanyang Technological University, Singapore, 637551, Singapore.
Yi Ling SeahSchool of Biological Sciences, Nanyang Technological University, Singapore, 637551, Singapore.
Charlie MarvalimSchool of Biological Sciences, Nanyang Technological University, Singapore, 637551, Singapore.
Guillaume ThibaultSchool of Biological Sciences, Nanyang Technological University, Singapore, 637551, Singapore. thibault@ntu.edu.sg.ORCID http://orcid.org/0000-0002-7926-4812
Nanyang Technological University · SG

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Phospholipid homeostasis in biological membranes is essential to maintain functions of organelles such as the endoplasmic reticulum. Phospholipid perturbation has been associated to cellular stress responses. However, in most cases, the implication of membrane lipid changes to homeostatic cellular response has not been clearly defined. Previously, we reported that Saccharomyces cerevisiae adapts to lipid bilayer stress by upregulating several protein quality control pathways such as the endoplasmic reticulum-associated degradation (ERAD) pathway and the unfolded protein response (UPR). Surprisingly, we observed certain ER-resident transmembrane proteins, which form part of the UPR programme, to be destabilised under lipid bilayer stress. Among these, the protein translocon subunit Sbh1 was prematurely degraded by membrane stiffening at the ER. Moreover, our findings suggest that the Doa10 complex recognises free Sbh1 that becomes increasingly accessible during lipid bilayer stress, perhaps due to the change in ER membrane properties. Premature removal of key ER-resident transmembrane proteins might be an underlying cause of chronic ER stress as a result of lipid bilayer stress.

Indexed as

Endoplasmic Reticulum-Associated DegradationEndoplasmic Reticulum StressCytosolLipid BilayersLysineMembrane FluidityMembrane LipidsMembrane ProteinsModels, BiologicalPhosphatidylcholinesPhospholipidsProtein BindingProtein DomainsProtein StabilitySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsLipid BilayersLysineMembrane LipidsMembrane ProteinsPhosphatidylcholinesPhospholipidsSaccharomyces cerevisiae Proteins

Identifiers

PMID31201345
PMCPMC6572771
OpenAlexW2953254812

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.