Evidence map›Paper›PMID 34857875›Full record

ArticleCommunications biology2021

ER-misfolded proteins become sequestered with mitochondria and impair mitochondrial function.

Adrián Cortés Sanchón, Harshitha Santhosh Kumar, Matilde Mantovani, Ivan Osinnii, José María Mateos, Andres Kaech, Dimitri Shcherbakov, Rashid Akbergenov, Erik C Böttger

Abstract read
In one paragraph

Article in Communications biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
–field-weighted citation impact
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

20 citing papers in PubMed.

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  18. Mitochondria inter-organelle relationships in cancer protein aggregation.Frontiers in cell and developmental biology · 2022
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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

9 authors.

Adrián Cortés Sanchón *Institut für Medizinische Mikrobiologie, Universität Zürich, 8006, Zurich, Switzerland.
Harshitha Santhosh Kumar *Institut für Medizinische Mikrobiologie, Universität Zürich, 8006, Zurich, Switzerland.
Matilde Mantovani *Institut für Medizinische Mikrobiologie, Universität Zürich, 8006, Zurich, Switzerland.
Ivan OsinniiInstitut für Medizinische Mikrobiologie, Universität Zürich, 8006, Zurich, Switzerland.
José María MateosCenter for Microscopy and Image Analysis, University of Zurich, 8057, Zurich, Switzerland.ORCID http://orcid.org/0000-0002-3675-6198
Andres KaechCenter for Microscopy and Image Analysis, University of Zurich, 8057, Zurich, Switzerland.
Dimitri ShcherbakovInstitut für Medizinische Mikrobiologie, Universität Zürich, 8006, Zurich, Switzerland.
Rashid AkbergenovInstitut für Medizinische Mikrobiologie, Universität Zürich, 8006, Zurich, Switzerland.
Erik C BöttgerInstitut für Medizinische Mikrobiologie, Universität Zürich, 8006, Zurich, Switzerland. boettger@imm.uzh.ch.ORCID http://orcid.org/0000-0002-2570-0121

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Proteostasis is a challenge for cellular organisms, as all known protein synthesis machineries are error-prone. Here we show by cell fractionation and microscopy studies that misfolded proteins formed in the endoplasmic reticulum can become associated with and partly transported into mitochondria, resulting in impaired mitochondrial function. Blocking the endoplasmic reticulum-mitochondria encounter structure (ERMES), but not the mitochondrial sorting and assembly machinery (SAM) or the mitochondrial surveillance pathway components Msp1 and Vms1, abrogated mitochondrial sequestration of ER-misfolded proteins. We term this mitochondria-associated proteostatic mechanism for ER-misfolded proteins ERAMS (ER-associated mitochondrial sequestration). We testify to the relevance of this pathway by using mutant α-1-antitrypsin as an example of a human disease-related misfolded ER protein, and we hypothesize that ERAMS plays a role in pathological features such as mitochondrial dysfunction.

Indexed as

Protein FoldingAdenosine TriphosphatasesCarrier ProteinsEndoplasmic ReticulumHEK293 CellsHumansMitochondriaSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAdenosine TriphosphatasesCarrier ProteinsMSP1 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsVms1 protein, S cerevisiae

Identifiers

PMID34857875
PMCPMC8640021

What OpenQuestion holds

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Registered trials

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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.