Evidence map›Paper›PMID 37311770›Full record

ArticleNature communications2023

TMX4-driven LINC complex disassembly and asymmetric autophagy of the nuclear envelope upon acute ER stress.

Marika K Kucińska, Juliette Fedry, Carmela Galli, Diego Morone, Andrea Raimondi, Tatiana Soldà, Friedrich Förster, Maurizio Molinari

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
9.2field-weighted citation impact, top 1% 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

29 citing papers in PubMed, 44 citations in OpenAlex.

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  19. Life outside the LINC complex - Do SUN proteins have LINC-independent functions?BioEssays : news and reviews in molecular, cellular and developmental biology · 2024
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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

8 authors at 5 institutions in 3 countries.

Marika K Kucińska *Università della Svizzera italiana (USI), Faculty of Biomedical Sciences, Institute for Research in Biomedicine, CH-6500, Bellinzona, Switzerland.
Juliette Fedry *Structural Biochemistry, Bijvoet Center for Biomolecular Research, Utrecht University, 3584 CG, Utrecht, The Netherlands.ORCID 0000-0002-6592-4269
Carmela GalliUniversità della Svizzera italiana (USI), Faculty of Biomedical Sciences, Institute for Research in Biomedicine, CH-6500, Bellinzona, Switzerland.
Diego MoroneUniversità della Svizzera italiana (USI), Faculty of Biomedical Sciences, Institute for Research in Biomedicine, CH-6500, Bellinzona, Switzerland.ORCID 0000-0002-6847-3811
Andrea RaimondiUniversità della Svizzera italiana (USI), Faculty of Biomedical Sciences, Institute for Research in Biomedicine, CH-6500, Bellinzona, Switzerland.
Tatiana SoldàUniversità della Svizzera italiana (USI), Faculty of Biomedical Sciences, Institute for Research in Biomedicine, CH-6500, Bellinzona, Switzerland.
Friedrich FörsterStructural Biochemistry, Bijvoet Center for Biomolecular Research, Utrecht University, 3584 CG, Utrecht, The Netherlands.ORCID 0000-0002-6044-2746
Maurizio MolinariUniversità della Svizzera italiana (USI), Faculty of Biomedical Sciences, Institute for Research in Biomedicine, CH-6500, Bellinzona, Switzerland. maurizio.molinari@irb.usi.ch.ORCID 0000-0002-7636-5829
École Polytechnique Fédérale de Lausanne · CHUniversità della Svizzera italiana · CHUtrecht University · NLUniversity of Bern · CHVita-Salute San Raffaele University · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The endoplasmic reticulum (ER) is an organelle of nucleated cells that produces proteins, lipids and oligosaccharides. ER volume and activity are increased upon induction of unfolded protein responses (UPR) and are reduced upon activation of ER-phagy programs. A specialized domain of the ER, the nuclear envelope (NE), protects the cell genome with two juxtaposed lipid bilayers, the inner and outer nuclear membranes (INM and ONM) separated by the perinuclear space (PNS). Here we report that expansion of the mammalian ER upon homeostatic perturbations results in TMX4 reductase-driven disassembly of the LINC complexes connecting INM and ONM and in ONM swelling. The physiologic distance between ONM and INM is restored, upon resolution of the ER stress, by asymmetric autophagy of the NE, which involves the LC3 lipidation machinery, the autophagy receptor SEC62 and the direct capture of ONM-derived vesicles by degradative LAMP1/RAB7-positive endolysosomes in a catabolic pathway mechanistically defined as micro-ONM-phagy.

Indexed as

Endoplasmic Reticulum StressNuclear EnvelopeAnimalsAutophagyEndoplasmic ReticulumMammalsUnfolded Protein Response

Identifiers

PMID37311770
PMCPMC10264389
OpenAlexW4380480552

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.