Evidence map›Paper›PMID 34831188›Full record

ReviewCells2021

The Unfolded Protein Response as a Guardian of the Secretory Pathway.

Toni Radanović, Robert Ernst

Open access · goldAbstract readReview
In one paragraph

Review in Cells, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
6.0field-weighted citation impact, top 2% 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

34 citing papers in PubMed, 65 citations in OpenAlex.

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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

2 authors at 1 institution in 1 country.

Toni RadanovićMedical Biochemistry and Molecular Biology, Medical Faculty, Saarland University, 66421 Homburg, Germany.
Robert ErnstMedical Biochemistry and Molecular Biology, Medical Faculty, Saarland University, 66421 Homburg, Germany.ORCID 0000-0002-0283-3490
Saarland University · DE

Funding

Deutsche Forschungsgemeinschaft SFB894, Ca2+-Signals: 686 Molecular Mechanisms and Integrative FunctionsEuropean Research Council CoG no. 866011Volkswagen Foundation Life? no. 93089
6 · The paper itself

Abstract

The endoplasmic reticulum (ER) is the major site of membrane biogenesis in most eukaryotic cells. As the entry point to the secretory pathway, it handles more than 10,000 different secretory and membrane proteins. The insertion of proteins into the membrane, their folding, and ER exit are affected by the lipid composition of the ER membrane and its collective membrane stiffness. The ER is also a hotspot of lipid biosynthesis including sterols, glycerophospholipids, ceramides and neural storage lipids. The unfolded protein response (UPR) bears an evolutionary conserved, dual sensitivity to both protein-folding imbalances in the ER lumen and aberrant compositions of the ER membrane, referred to as lipid bilayer stress (LBS). Through transcriptional and non-transcriptional mechanisms, the UPR upregulates the protein folding capacity of the ER and balances the production of proteins and lipids to maintain a functional secretory pathway. In this review, we discuss how UPR transducers sense unfolded proteins and LBS with a particular focus on their role as guardians of the secretory pathway.

Indexed as

Secretory PathwayUnfolded Protein ResponseAnimalsHumansLipid BilayersModels, BiologicalProteostasisStress, PhysiologicalLipid BilayersATF6ERhydrophobic mismatchIRE1lipid bilayer stressmembrane stiffnessmembrane thicknessPERKproteotoxic stresssecretory pathwayUPR

Identifiers

PMID34831188
PMCPMC8616143
OpenAlexW3210859979

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.